3462|"The disulfide bridges of the trypsin-kallikrein inhibitor K from snails (Helix pomatia).
3462|Two cystine-containing peptides with the disulfide bridges Cys32-Cys53 and Cys32-Cys53 plus Cys7-Cys57 were obtained after thermolytic hydrolysis of the native inhibitor at 80 degrees C and chromatographic separation of the peptides using SE-Sephadex.
3462|The Cys16-Cys40 disulfide bridge could be reduced selectively by sodium borohydride with no loss in biological activity.
30689|"The disulfide bridges of toxin II from Anemonia sulcata."
393607|Purification and characterization of the disulfide bridges."
393607|It is shown that the subunits of the polymers are covalently attached through either Cysl3, Cysl7 or both these residues of the H-chain.
438159|"Identification of the interchain disulfide bonds of dimeric human placental lactogen."
444453|"Structure of potato carboxypeptidase inhibitor: disulfide pairing and exposure of aromatic residues."
444453|Since the native inhibitor is resistant to fragmentation by proteases, the protein was first subjected to cleavage at aspartic acid residues by exposure to 0.03 N HCl at 110 degrees C for 10h to yield a fragment containing two chains (residues 6-15 and residues 18-39)held together by three disulfide bonds.
444453|Digestion with subtilisin and Pronase, respectively, yielded sets of peptides from which, by diagonal electrophoresis and amino acid analysis, the paired cystinyl residues were identified as Cys-8 to Cys-24, Cys-12 to Cys-27, and Cys-18 to Cys-34.
534646|"Intrachain disulfide bridges of bovine seminal ribonuclease."
712836|"Three-dimensional structure and disulfide bond connections in bovine pancreatic phospholipase A2."
887933|"Relaxin: a disulfide homolog of insulin."
891553|Characterization of disulfide-containing cyanogen-bromide fragments."
936108|"Disulfide bridges in nh2 -terminal part of human fibrinogen."
1002129|"Rule of antibody structure. the primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie), I: Purification and characterization of the protein, the L- and H-chains, the cyanogenbromide cleavage products, and the disulfide bridges."
1148181|The cardiotoxin, molecular weight 6806 from amino acid composition, consists of 60 amino acids, cross-linked by four disulfide bridges, connecting 3-21, 14-38, 42-53, and 54-59.
1148181|A partial reduction experiment in the absence of denaturing agent using 14-C-labeled iodoacetic acid as S-carboxymethylating agent shows that disulfide bonds 14-38 and 42-53 were reduced fastest followed marginally by 54-59, and then bond 3-21.
1201911|Disulfide bridges of the beta subunit."
1201911|Results indicate that the disulfide bridges are formed by residues 9-38, 23-72, 26-110, 34-90, 57-88, and 93-100.
1225902|"The disulfide bridges of ribonuclease U2 from Ustilago sphaerogena."
1225902|From the results of amino acid analysis of cystine-containing peptides and their oxidized components, the three disulfide bridges were located between the cystine residues at positions 1 and 53, 9 and 112, and 54 and 95.
1281423|"Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP."
1281423|We determined the state of all cysteine residues and localized four of them as free thiols at positions 24, 32, 34, and 168.
1281423|Four cysteines are connected by disulfide bonds: Cys200-Cys219 and Cys183-Cys227.
1303747|"Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active site segments."
1303747|Analysis of fragments obtained from the native enzyme after digestion with pepsin identified bridges connecting Cys-98 with Cys-125, and Cys-166 with Cys-200.
1304918|"The disulfide bond pairing of the pheromones Er-1 and Er-2 of the ciliated protozoan Euplotes raikovi."
1304918|The same pairing, Cys(I)-Cys(IV), Cys(II)-Cys(VI), and Cys(III)-Cys(V), was found in both pheromones, suggesting that this pattern occurs commonly throughout this family of molecules.
1317862|"Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF."
1317862|Using an approach involving partial reduction of PDGF, we have identified the 2nd and 4th cysteine residues in the PDGF chains as the cysteine residues forming interchain disulfide bonds.
1317862|Analysis of PDGF mutants in which the 2nd and 4th cysteine residues were mutated to serine residues revealed that the disulfide bonds are arranged in a cross-wise manner, with the 2nd cysteine residue in one chain being linked to the 4th cysteine residue in the other.
1377029|"Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen)."
1377029|From sequence analyses of these peptides, we could identify all disulfide bonds in the 4 SCR units of DAF as being between the first and the third and between the second and the fourth half-cystines within each SCR unit.
1390663|Three disulfide bridges have been localized as Cys31-Cys63, Cys52-Cys86, and Cys66-Cys123 both by 1H nuclear magnetic resonance spectroscopy and by plasma desorption mass spectrometry.
1417742|The positions of the two disulphide bonds in the IgE-binding region were also determined: residue 110 is joined to residue 124, and residue 42 to residue 133.
1421801|"Synthesis and disulfide structure determination of agelenin: identification of the carboxy-terminus as an amide form."
1421801|The disulfide structure of agelenin was also determined to be linked between 3-19, 10-24 and 18-34, by comparing the tryptic peptide linked by two disulfide bonds with those synthesized by the selective formation of disulfide bonds.
1426288|"Activity, disulphide mapping and structural modelling of the fifth domain of human beta 2-glycoprotein I."
1426288|In an attempt to define the 3D structure of this domain, the disulphide linkage pattern was determined and shown to be Cys 1-4, Cys 2-5 and Cys 3-6 in contradiction to an earlier report.
1445902|"Determination of the glycosylation patterns, disulfide linkages, and protein heterogeneities of baculovirus-expressed mouse interleukin-3 by mass spectrometry."
1445902|Liquid secondary ion mass spectrometric analysis of the unreduced tryptic peptides provided evidence for disulfide linkages between Cys-140 and Cys-79 or Cys-80 and between Cys-17 and Cys-79 or Cys-80.
1445902|In comparison to the major component, a minor IL-3 species (M(r) 17-19 x 10(3) by SDS-PAGE) isolated from the hemolymph showed no difference with respect to the glycosylation pattern or the disulfide linkages, but it was cleaved between Ala-127 and Ser-128, and only a disulfide linkage between Cys-140 and Cys-79 or Cys-80 held the molecule together.(
1472036|"Identification of a disulfide bridge connecting the alpha-subunits of the extracellular domain of the insulin receptor."
1472036|The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524.
1472036|The peptides containing Cys435 and Cys468 appeared in the same fraction, indicating that these two form a disulfide bond, and in another fraction we found the sequence of the peptide containing Cys524.
1472036|Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit.
1472500|"Disulfide bond assignment in human J chain and its covalent pairing with immunoglobulin M."
1472500|We show that in J chain the three intradisulfide bridges are formed between Cys 12 and 100, Cys 71 and 91, and Cys 108 and 133.
1472500|Previous reports [reviewed by Koshland, M. E. (1985) Annu. Rev. Immunol. 3, 425-453] have proposed that cysteines 12, 14, or 68 were linked to the penultimate cysteine 575 of two mu chain tails.
1472500|In this work, we demonstrate that cysteines 14 and 68 are disulfide-bridged to mu chains.
1491011|"Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J)."
1491011|Disulfide bonds thus determined were between Cys58(alpha)-Cys107(beta), Cys68(alpha)-Cys99(beta), Cys75(alpha)-Cys94(beta), and Cys86(alpha)-Cys80(beta).
1491011|Since there was no free sulfhydryl groups in the SP-40,40 molecule, Cys78(alpha) and Cys91(beta) should also be linked by a disulfide bond.
1515030|"Determination of disulfide bond arrangement in bombyxin-IV, an insulin superfamily peptide from the silkworm, Bombyx mori, by combination of thermolysin digestion of natural peptide and selective synthesis of disulfide bond isomers."
1515030|Two other isomers with respect to disulfide bond arrangement, [A6-A7, A11-B10, A20-B22-cystine]- and [A6-B10, A7-A11, A20-B22-cystine]-bombyxin-IVs, were distinguishable from the natural one by use of HPLC, thermolysin digestion, and bioassay.
1516704|"The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin."
1516704|In flavoridin, direct evidence for the existence of linkage between Cys4-Cys19 and between Cys45 and Cys64 was obtained by analysis of proteolytic products, and indirect evidence suggests links between Cys6-Cys14 and Cys13-Cys36.
1516704|In echistatin, links between Cys8-Cys37 and Cys20-Cys39 were identified by direct chemical analysis.
1551440|"SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges."
1567819|"Complete primary structure of bovine beta 2-glycoprotein I: localization of the disulfide bridges."
1567819|In the four N-terminal domains, the first and third and the second and fourth half-cystines are disulfide-linked, while in the fifth domain the first and fourth, the second and fifth, and the third and sixth half-cystines are disulfide-linked.
1568474|Disulfide bridges, C-terminal end, and peptide analysis of the airway form."
1568474|Three intrachain disulfide bridges were defined, linking Cys8 to Cys77, Cys11 to Cys71 and Cys35 to Cys46.
1568474|The remaining Cys48 is concluded to link the protein chains into homodimers via an interchain disulfide to its counterpart in a second SP-B polypeptide.
1576156|Both GHs consist of 190 amino acid residues, and contain two disulfide linkages at positions 52-163 and 180-188.
1628650|"The multimeric structure and disulfide-bonding pattern of bovine kappa-casein."
1628650|Three types of interchain disulfide linkage, Cys11-Cys11, Cys11-Cys88 and Cys88-Cys88, were all assigned in multimers purified from [14C]carboxymethylated and untreated bulk milk, as well as a milk sample from a kappa-casein-variant-B homozygote Co20.
1632791|"The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket."
1632791|Analysis of purified bovine tropoelastin with Ellman's reagent and [14C]iodoacetamide demonstrated that the only two cysteine residues in the molecule form an intrachain disulfide bond.
1634328|Assignment of disulfide bond location."
1634328|We elucidated the complete structure of Manduca EH as a 62-residue peptide which has three disulfide bonds between Cys14-Cys38, Cys18-Cys34, and Cys21-Cys49.
1644794|Disulfide bonds and similarity to lectin-binding proteins."
1644794|We have analyzed these half-cystine residues and established that all 10 of the half-cystine residues appeared to be involved in disulfide bond formation and that disulfide bonds linked Cys7 to Cys18, Cys35 to Cys125, and Cys89 to Cys117.
1644794|Possible arrangements of the two remaining disulfide bonds include linkages Cys69/111 to Cys100/101.
1644794|Two of the disulfide linkages we determined for sea raven AFP: Cys7-Cys18 and Cys35-Cys125, are conserved in these proteins.
1645336|"Disulfide pairing of the recombinant kringle-2 domain of tissue plasminogen activator produced in Escherichia coli."
1645336|Five major peptides containing 35S were obtained. Amino acid sequence analysis showed that these peptides represented various cleavage products containing one or more of the following disulfides: Cys180-Cys261, Cys201-Cys243, Cys232-Cys256 (sequence numbering based on Pennica et al. (Pennica, D., Holmes, W.E., Kohr, W.J., Hakins, R.N., Vehar, G. A., Ward, C.A., Bennett, W.F., Yelverton E., Seeburg, P.H., Heynecker, H.L., Goeddel, E.V., and Collen, D. (1983) Nature 301, 214-221)).
1648964|"Surfactant protein B: disulfide bridges, structural properties, and kringle similarities."
1648964|Results show that three intrachain bridges link half-cystine residues 8 and 77, 11 and 71, and 35 and 46, respectively.
1648964|In the major form of SP-B, the remaining half-cystine, Cys-48, is probably interchain-linked to its counterpart in another molecule, compatible with the existence of dimeric molecules.
1648964|A minor fraction, with monomeric SP-B but also lacking free thiols, could be due to polypeptides having Cys-57 (instead of Leu in the major form) and hence an additional intrachain bond (Cys-48-Cys-57).
1651718|"Connexon integrity is maintained by non-covalent bonds: intramolecular disulfide bonds link the extracellular domains in rat connexin-43."
1688430|"Role of disulfide bond formation in the folding of human chorionic gonadotropin beta subunit into an alpha beta dimer assembly-competent form."
1688430|The last three disulfide bonds to form are those between cysteines 9 and 90, 23 and 72, and 93 and 100.
1699936|The 1-37-amino acid hexasulfhydryl peptide oxidizes readily to give the tricyclic disulfide structure in good yield.
1699936|Analysis of the sequence and amino acid composition of the resulting fragments defines a disulfide bond arrangement (Cys7-Cys28, Cys13-Cys33, Cys17-Cys35) which differs from that previously suggested.
1703542|"The myelin-associated glycoproteins: membrane disposition, evidence of a novel disulfide linkage between immunoglobulin-like domains, and posttranslational palmitylation."
1707134|The third chain, C8 gamma, is covalently linked to C8 alpha by a disulfide linkage; it is demonstrated that Cys40 of C8 gamma is linked to Cys164 of C8 alpha, a unique cysteine located in a loop located between the cysteine-rich LDL-receptor class A module and the membrane-inserting region of C8 alpha.
1708771|The four cysteines form two intramolecular disulfide bonds, Cys4-Cys89 and Cys43-Cys138.
1730242|"Localization of the intrachain disulfide bonds of the envelope glycoprotein 71 from Friend murine leukemia virus."
1730242|The first cysteine residue of the sequence (Cys46) was shown to be coupled to the sixth (Cys98), leading to a large loop containing four additional cysteine residues.
1730242|Computer model building and energy calculations led to the assignment of Cys72 to Cys87 and Cys73 to Cys83.
1730242|The following four cysteine residues of the sequence also constitute a structural unit, with Cys121 bonded to Cys141 and Cys133 to Cys146, and the last two cysteine residues in the amino-terminal domain of glycoprotein 71 form a small loop (Cys178 to Cys184).
1730242|The first two cysteine residues of the carboxy-terminal domain produce a very small hydrophobic loop (Cys312-Cys315).
1730242|Cys361 is bound to Cys373, Cys342 to Cys396 and Cys403 to Cys416.
1751487|"Amino acid sequence and location of the disulfide bonds in bovine beta 2 glycoprotein I: the presence of five Sushi domains."
1756858|"Determination of the amino acid sequence of an intramolecular disulfide linkage-containing sperm-activating peptide by tandem mass spectrometry."
1827035|A disulfide bond between Cys83 and Cys91 was identified by isolation of tryptic peptides bearing a fluorescent label, IAEDANS, from wild-type and C91 V enzymes followed by amino acid sequencing.
1832834|"Location of the disulfide bonds in the antitumor protein neocarzinostatin."
1832834|Sequence analyses of the isolated peptides revealed the location of the disulfide bonds at Cys37-Cys47 and Cys88-Cys93.
1856193|"Determination of disulfide bond pairs and stability in recombinant tick anticoagulant peptide."
1856193|The specific disulfide bridges, Cys-5 to Cys-59, Cys-15 to Cys-39, and Cys-33 to Cys-55, are analogous to those in the prototype Kunitz-type inhibitor, bovine pancreatic trypsin inhibitor (BPTI).
1868845|"Assignment of the five disulfide bridges in an alpha-amylase inhibitor from wheat kernel by fast-atom-bombardment mass spectrometry and Edman degradation."
1898734|Sequence locations of alpha-lactalbumin binding site, thiol groups, and disulfide bond."
1898734|From their lack of reactivity it is deduced that the remaining two cysteines, residues 134 and 247, are joined in a disulfide linkage.
1898734|From these results and those of a previous study of UDP-galactose binding (Yadav, S., and Brew, K. (1990) J. Biol. Chem. 265, 14163-14169) it appears that the soluble form of galactosyltransferase is composed of two domains, the NH2-terminal 150 residues containing the Cys134-Cys247 disulfide bond, which functions in alpha-lactalbumin and acceptor binding, and the COOH-terminal region, which is involved in UDP-galactose binding.
1911854|"Determination of disulfide array and subunit structure of taste-modifying protein, miraculin."
1911854|The formation of three intrachain disulfide bridges at Cys-47-Cys-92, Cys-148-Cys-159 and Cys-152-Cys-155 and one interchain disulfide bridge at Cys-138 was determined by amino acid sequencing and composition analysis of cystine-containing peptides isolated by HPLC.
1917966|"Carbohydrate-binding protein 35 (Mac-2), a laminin-binding lectin, forms functional dimers using cysteine 186."
1917966|Site-directed mutagenesis indicated that cysteine 186, the single cysteine residue in CBP35, is required for dimerization.
1936247|Location of disulphide bridges."
1986782|"Primary structure and analysis of the location of the regulatory disulfide bond of pea chloroplast NADP-malate dehydrogenase."
1986782|Using digestion products of NADP-malate dehydrogenase with aminopeptidase K, the location of the single disulfide bridge was established to be on the N-terminal arm (Cys-12 and Cys-17) of the polypeptide chain.
1988019|"Identification of bull protamine disulfides."
1988451|"Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane."
1988451|Our studies show that Cys22 and Cys38 form an intrasubunit disulfide bond which contributes to the heat stability of the LamB protein trimer.
1989985|"Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase."
1989985|The identical monomer chains of the dimeric native enzyme are found to contain three disulfide bonds, specifically Cys-129 to Cys-340, Cys-183 to Cys-281, and Cys-315 to Cys-319.
1993171|"Disulfide assignments in recombinant mouse and human interleukin 4."
1993171|For mouse IL-4, the first and fifth, second and fourth, and third and sixth cysteines are joined.
1993171|The disulfide bonds in human IL-4 are between the first and sixth, second and fourth, and third and fifth cysteines.
1998666|"Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule."
1998666|The apple domains (90 or 91 amino acids) contain 3 highly conserved disulfide bonds linking the first and sixth, second and fifth, and third and fourth half-cystine residues present in each repeat.
1998667|"Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains."
1998667|The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
2001252|"Assignment of disulphide bonds in human platelet GPIIIa.
2001252|A disulphide pattern for the beta-subunits of the integrin family."
2001252|We also assign unambiguously the disulphide bonds within the N-terminal, the fibrinogen-binding and the C-terminal domains, and the two long-range disulphide bonds which join the N-terminus to the proteinase-resistant core (Cys5-Cys435) and the fibrinogen-binding domain to the extracellular side of the C-terminal domain (Cys406-Cys655).
2007122|"Identification of the disulfide bonds of human complement C1s."
2007122|All of the 26 half-cystines are linked in disulfide bonds occurring at positions 50-68, 120-132, 128-141, 143-156, 160-187, 219-236, 279-326, 306-339, 344-388, 371-406, 410-534, 580-603, and 613-644.
2013293|"Determination of disulfide bridges in natural and recombinant insect defensin A."
2026606|"Disulfide bond assignment and identification of regions required for functional activity of oncostatin M."
2026606|Two intramolecular disulfide bonds, C6-C127 and C49-C167, were identified in recombinant oncostatin M.
2026606|Taken together, these results indicate that biological activity of oncostatin M requires discontinuous regions of the molecule, including residues near the essential disulfide bond, C49-C167, and within a putative amphiphilic helix at the carboxyl terminus.
2036389|"Identification of the disulfide bond pattern in albolabrin, an RGD-containing peptide from the venom of Trimeresurus albolabris: significance for the expression of platelet aggregation inhibitory activity."
2037074|"Human interleukin-5 expressed in Escherichia coli: assignment of the disulfide bridges of the purified unglycosylated protein."
2037074|Disulfide linked peptides containing cysteine 42 linked to cysteine 84 were isolated.
2037074|This indicated that cysteines 42 and 84 of one subunit were linked in an antiparallel manner to cysteines 84 and 42 of the other subunit.
2070794|"Identification of the disulphide bonds in human platelet glycocalicin."
2070794|The position and linkage of these two disulphide bonds are now determined to be 209-248 and 211-264 and the relevance of this double-loop structure for glycoprotein Ib/IX function is discussed.
2080919|"Studies on the disulfide bridges of sarafotoxins.
2080919|Chemical synthesis of sarafotoxin S6B and its homologue with different disulfide bridges."
2081731|HT-2 consisted of 202 amino acid residues with two disulfide bridges, which were assigned to Cys-117-Cys-197 and Cys-157-Cys-164.
2108021|"Arrangement of disulfide bridges and positions of sulfhydryl groups in tetanus toxin."
2108021|It was established that the half-cystine residues in positions 26, 185, 198, 311, 868, and 1300 are present in the sulfhydryl form, that those in positions 438 and 466 are disulfide-bridged, thereby connecting the light and heavy chains of the toxin, and that those in positions 1076 and 1092 are disulfide-bridged, thereby giving rise to a loop in the heavy chain.
2111316|"Disulfide bridge structure of ascidian trypsin inhibitor I: similarity to Kazal-type inhibitors."
2145276|"Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187."
2145276|The C110-C187 disulfide bond is buried in rhodopsin because reactions with disulfide reducing agents and cyanide ion require prior treatment with denaturants.
2163605|"Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)."
2163605|This procedure allowed the direct assignment of Cys-145-Cys-166 and the isolation of two other peptides containing two disulphide bonds each.
2163605|Further peptide cleavage in conjunction with fast-atom-bombardment m.s. analysis permitted the assignments Cys-1-Cys-70, Cys-3-Cys-99, Cys-13-Cys-124 and Cys-127-Cys-174 from these peptides.
2163605|The sixth bond Cys-132-Cys-137 was assigned by inference, as the native protein has no detectable free thiol groups.
2171523|"Four disulfide bonds' allocation of Na+, K(+)-ATPase inhibitor (SPAI)."
2171523|The four cysteine pairs were disclosed to be Cys20 to Cys49, Cys27 to Cys53, Cys36 to Cys48, and Cys42 to Cys57, all linked by disulfide bridge formation.
2223768|All cysteines are engaged as disulfide bonds: Cys(13)-Cys(59), Cys(48)-Cys(66), and Cys(79)-Cys(146).
2226447|"Amino acid sequence and disulfide bridges of an antifungal protein isolated from Aspergillus giganteus."
2226447|Disulfide bonds were formed between Cys7-Cys33, Cys14-Cys40, Cys26-Cys28 and Cys49-Cys51.
2229005|Four disulfide bonds link half-cystinyl residue 19 to 72, 34 to 82, 52 to 97, and 94 to 111.
2261983|"Complete localization of the disulfide bridges and glycosylation sites in boar sperm acrosin."
2266134|cDNA cloning, disulfide locations, and subcellular localization."
2332434|"The disulfide structure of mouse lysosome-associated membrane protein 1."
2332434|NH2-terminal sequencing as well as reduction, alkylation, and rechromatography of the disulfide-linked fragments led to the following assignment of disulfide bonds: Cys11 and Cys50, Cys125 and Cys161, Cys198 and Cys235, and Cys303 and Cys340.
2332434|The loops formed by the Cys11-Cys50 and Cys198-Cys235 bridges are homologous, and the Cys125-Cys161 and Cys303-cys340 loops form a second set of homologous domains.
2338142|"Disulfide pairings in geographutoxin I, a peptide neurotoxin from Conus geographus."
2338142|The disulfide bridges were found to be between Cys3 and Cys15, Cys4 and Cys20, and Cys21, indicating that geographutoxin I has a rigid conformation consisting of three loops stabilized by these three disulfide linkages.
2354201|"The positions of the disulfide bonds and the glycosylation site in a lectin of the acorn barnacle Megabalanus rosa."
2354201|One intrachain and two interchain disulfide bonds were identified as Cys-53-Cys-61, Cys-14-Cys-50' and Cys-50-Cys-14', respectively, by enzymatic digestion and Edman degradation of CB1.
2354201|Two intrachain disulfide bonds were determined as Cys-78-Cys-168 and Cys-144-Cys-160 by enzymatic digestion of CB2.
2355006|"Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells."
2358424|"Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly)."
2358424|Results showed that sapecin has a vortical structure fixed by 3 disulfide bonds between cysteine residues 3 and 30, 16 and 36, and 20 and 38, respectively, and that these disulfide bonds are essential for its antibacterial activity.
2361960|The analyses of sulfhydryl content in rhIL-5 molecule and disulfide-containing peptide obtained from API digestion indicated that active form of rhIL-5 existed as an antiparallel dimer linked by two pairs of Cys-44 and Cys-86.
2390214|"Disulfide bridges of bovine spleen cathepsin B."
2390214|Disulfide bridges link together Cys14-Cys43, Cys26-Cys71, Cys62-Cys128, Cys63-Cys67, Cys100-Cys132, Cys108-Cys119 and Cys148-Cys252.
2406245|Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain."
2406245|Peptide mapping studies show these disulfides are paired sequentially to produce short loops (10-15 residues long) as follows: Cys38-Cys48, Cys83-Cys94, and Cys108-Cys122.
2472117|"Disulfide structures of human interleukin-6 are similar to those of human granulocyte colony stimulating factor."
2472117|By isolation and characterization of tryptic and subtilytic peptides obtained from different proteolytic digestions, the disulfide bonds of the IL-6 molecule were assigned to Cys44-Cys50 and Cys73-Cys83.
2473918|"Identification of thiol groups and a disulfide crosslink site in bovine myelin proteolipid protein."
2473918|These experiments showed that Cys-32 and Cys-34 are free thiols, and are presumably on the interior of the cell or within the membrane bilayer, and that Cys-200 and Cys-219 are joined by a disulfide bond, and are probably located on the extracellular face of the membrane.
2514185|The disulfide linkages for polyphemusin I consisted of two bridges between Cys-4 and Cys-17 and between Cys-8 and Cys-13, which was identical to in the case of tachyplesin I.
2546555|"Identification of a disulfide between cysteine 214 and cysteine 277 in the beta subunit of native (Na+ + K+)ATPase."
2546555|The disulfide is between Cysteine 214 and Cysteine 277.
2573358|"Disulfide bonds in neurotoxin-III from the sea anenome Radianthus macrodactylus."
2573358|Positions of the three disulfide bridges in neurotoxin-III (RTX-III) from sea anemone Radianthus macrodactylus were determined: Cys3--Cys43, Cys5--Cys33, Cys26--Cys44.
2584229|Assignment of disulfide bonds and visualization of its domain arrangement."
2645941|"The position of the disulfide bonds in human plasma alpha 2 HS-glycoprotein and the repeating double disulfide bonds in the domain structure."
2645941|One inter-disulfide bond containing peptide and five intra-disulfide bond containing peptides (A-chain) were purified and identified as Cys-18 (B-chain)--Cys-14 (A-chain), Cys-71--Cys-82, Cys-96--Cys-114, Cys-128--Cys-131, Cys-190--Cys-201 and Cys-212--Cys-229, respectively.
2674142|They are formed between Cys29 and Cys42, Cys218 and Cys241, Cys266 and Cys285, Cys277, and Cys280, and Cys420 and Cys440.
2722836|"Structure and activity dependence of recombinant human insulin-like growth factor II on disulfide bond pairing."
2738047|"Amino acid sequences and disulfide bridges of serine proteinase inhibitors from bitter gourd (Momordica charantia LINN.) seeds."
2760022|One of the three disulfide bonds exists between Cys12 and Cys28, and the two others links Cys32-Cys33 with Cys6 and Cys16.
2760061|"The arrangement of disulfide loops in human alpha 2-HS glycoprotein.
2760061|Similarity to the disulfide bridge structures of cystatins and kininogens."
2760061|The first and the last half-cystine residues of the amino acid sequence of alpha 2-HS glycoprotein are engaged in the formation of a loop spanning the extreme NH2- and COOH-terminal portions of the molecule, thereby connecting the heavy and light chains.
2775232|"Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb."
2775232|It could be established that each cysteine residue in GPIIb, beginning at alpha-Cys-56, is disulphide-bonded to its nearest neighbour in the amino acid sequence.
2844531|"The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement-membrane type IV collagen."
2844531|In subdomain I, cysteines at positions 20 and 53 are connected with the C-terminal cysteine pair 108 and 111.
2844531|Thus formed, the disulfide knot stabilizes two interconnected loops of 32 and 54 residues, respectively.
2844531|A smaller loop of five residues occurs due to a disulfide bond between the cysteines 65 and 71.
2866794|Three disulfide bonds link the half-cystinyl residues 26-81, 39-92, and 57-107.
2880847|Cys50 and Cys74 and Cys313 and Cys356 were identified as the two disulfide bridges while the free sulfhydryl groups were located at positions 31 and 184.
2917986|"Determination of the disulfide array in the human defensin HNP-2.
2920839|Cys-18 and Cys-42 form a disulfide bridge.
2930486|"The occurrence of disulphide bonds in purified clathrin light chains."
3086886|"Partial primary structure of the T4 antigens of mouse and sheep: assignment of intrachain disulfide bonds."
3115973|"Location of disulfide bonds within the sequence of human serum cholinesterase."
3115973|Six of these form three internal disulfide bridges: between Cys65-Cys92, Cys252-Cys263, and Cys400-Cys519.
3115973|Cys571 forms a disulfide bridge with Cys571 of an identical subunit.
3138115|Both PrP isoforms were found to contain an intramolecular disulfide bond, linking Cys 179 and 214, which creates a loop of 36 amino acids containing the two N-linked glycosylation sites.
3166978|"Human tissue factor contains thioester-linked palmitate and stearate on the cytoplasmic half-cystine."
3166978|The extracellular disulfide cross-links, Cys49-Cys57 and Cys186-Cys209, were deduced from the analysis of tryptic peptides.
3192547|"Novel S-S loops in the giant hemoglobin of Tylorrhynchus heterochaetus."
3192547|The sites of disulfide bonds in the trimer have now been determined.
3242681|"Location of disulphide bonds in human insulin-like growth factors (IGFs) synthesized by recombinant DNA technology."
3242681|C6----C48, C47----C52 and C18----C61 assignments have been previously proposed for the three disulphide bonds linking six cysteine residues (C6, C18, C47, C48, C52 and C61), on the basis of analogy (and homology) with proinsulin.
3242681|This immediately established the C18----C61 linkage as it was contained in a singly bridged two-chain peptide.
3242681|The two other S-S bonds, which cross-link C6 and the 'tight' C47 to C52 segment, remained 'unresolved' within a more complex, doubly bridged triple-chain peptide.
3242681|Thirdly, further degradation of this structural block, in which cleavage of the C47-C48 bond was required to discern these bonds, was carried out by using FAB tandem mass spectrometry and (for additional corroboration) manual Edman degradation.
3242681|Both procedures confirmed the original C6----C48/C47----C52 prediction.
3264160|"Characterization of a recombinant murine interleukin-6: assignment of disulfide bonds."
3264160|It has been shown that there are disulfide bonds between Cys46-Cys52 and Cys75-Cys85.
3318813|The four Cys residues were found to be involved in two intramolecular disulphide bonds, linking the first and third, and second and fourth Cys residues.
3484639|"Complete amino acid sequence and location of the five disulfide bridges in porcine pancreatic alpha-amylase."
3502076|"Identification of disulfide-bridged substructures within human von Willebrand factor."
3519215|"Amino acid sequence and disulfide bridges of subunit III, a defective endopeptidase present in the bovine pancreatic 6 S procarboxypeptidase A complex."
3549683|"Role of disulfide bonds in the oligomeric structure and protease resistance of recombinant and native Treponema pallidum surface antigen 4D."
3552731|"Mode of disulfide bond formation of a heat-stable enterotoxin (STh) produced by a human strain of enterotoxigenic Escherichia coli."
3552731|Synthesis of the peptide with different modes of disulfide bond formation provided three peptides consistent with standard STh(6-18) in their physicochemical and biological properties, thereby indicating that the disulfide bonds in STh(6-18) are Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Thr-Gly-Cys.
3571203|Amino acid analyses and amino acid sequence analyses of the reduced pyridylethylated derivatives of the cystine peptides showed that seven of the disulfide bonds were as follows: Cys(24)-Cys(73), Cys(57)-Cys(138), Cys(64)-Cys(110), Cys(99)-Cys(169), Cys(116)-Cys(134), Cys(103)-Cys(152), Cys(167)-Cys(202).
3571203|The other two disulfide bonds were either Cys(5)-Cys(32) and Cys(33)-Cys(77) or Cys(5)-Cys(33) and Cys(32)-Cys(77).
3667618|Disulfide bonds were found to exist exclusively between Cys-16 and Cys-37, and this assignment, thus, establishes a general antiparallel alignment of the two chains.
3722144|"Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues."
3722144|Previously we showed that in intact receptor from Torpedo californica electric tissue reduction of this disulfide followed by affinity alkylation with 4-(N-maleimido)benzyltri[3H] methylammonium iodide specifically and uniquely labels the alpha subunit residues Cys-192 and Cys-193.
3722144|To identify all of the half-cystinyl residues contributing to the binding site disulfide(s), we have now reduced receptor under mild conditions and alkylated with a mixture of 4-(N-maleimido)benzyltri[3H]methylammonium iodide and N-[1-14C]ethylmaleimide and find that Cys-192 and Cys-193 are labeled exclusively.
3722144|Furthermore, from unreduced receptor we have isolated two cyanogen bromide peptides of alpha, one containing Cys-192 and Cys-193, and the other containing Cys-128 and Cys-142 (which are the other potential contributors to the binding site disulfide(s].
3722144|Our results demonstrate that: 1) the binding site disulfide is between Cys-192 and Cys-193; 2) Cys-128 is disulfide-cross-linked to Cys-142; and 3) under conditions that reduce Cys-192 and Cys-193 completely, Cys-128 and Cys-142 remain cross-linked.
3722144|We suggest that a transition between two stable conformations of the vicinal disulfide, both involving a nonplanar cis peptide bond between Cys-192 and Cys-193, is associated with receptor activation by agonists.
3759980|"Profile of the disulfide bonds in acetylcholinesterase."
3759980|The inter- and intrasubunit disulfide bridges for the 11 S form of acetylcholinesterase isolated from Torpedo californica have been identified.
3759980|These were localized in the polypeptide chain based on the cDNA-deduced sequence of the protein and were identified as Cys67-Cys94, Cys254-Cys265, and Cys402-Cys521.
3759980|Cys572, located in the carboxyl-terminal tryptic peptide, was disulfide-bonded to an identical peptide and most likely forms an intersubunit cross-link.
3779030|"Synthesis and secondary-structure determination of omega-conotoxin GVIA: a 27-peptide with three intramolecular disulfide bonds."
3782104|One of the two disulfide loops links Cys-101 and Cys-104 and the other Cys-173 and Cys-209.
3811228|"Analysis of disulfides present in the membrane proteins of the West Nile flavivirus."
3811228|The six disulfide bridges generated from the 12 cysteine residues in the WN virus-derived E protein have been identified as follows: Cys 1-Cys 2; Cys 3-Cys 8; Cys 4-Cys 6; Cys 5-Cys 7; Cys 9-Cys 10; Cys 11-Cys 12.
3875608|One of the disulfide bridges was found to be located between Cys(6) and Cys(22), and the other between Cys(40) and Cys(67) from the results of structure analyses of the two cystine-containing peptides obtained from the thermolysin digest of the native inhibitor.
4030947|Amino acid analysis of the fragments, generated from trypsin and V8 protease digestion of the 1 to 77 fragment, permitted assignment of cystine bridges between residues 2 and 24 and between residues 8 and 20.
4436313|Subunit structure and sequence location of the intrasubunit disulfide bond."
4448287|"Proceedings: The disulphide bridges of porcine luteinizing hormone alpha subunit."
4564211|"Covalent structure of bovine neurophysin-II: localization of the disulfide bonds."
4565406|Identification of the disulfide bridges."
4569282|"Location of sulfhydryl and disulfide groups in bovine -lactoglobulins and effects of urea."
4573324|"Studies on the interchain disulfides of human haptoglobins."
4580844|"The disulfide bridges of duck egg-white lysozyme II."
4603214|"The disulfide bonds of alpha1-acid glycoprotein."
4603223|The disulfide bridges."
4606908|The disulphide bonds."
4607177|"The disulphide bonds of viscotoxin A2 from the European mistletoe (Viscum album L. Loranthaceae)."
4611766|"Disulfide bonds of toxin II of the scorpion Androctonus australis Hector."
4614976|"The disulphide bridges of phospholipase A2 from bee venom."
4672150|"Disulfide bridges of the secretory trypsin inhibitor from procine pancreas and the degradation of covalent structure during the temporary inhibition."
4674343|"Localization of the four disulfide bridges in cytotoxin II from the venom of the indian cobra (Naja naja)."
4750422|Location of disulfide bonds."
4761089|"Interchain disulfide bridges in ribonuclease BS-1."
4797072|Disulfide bridges in soybean Bowman-Birk proteinase inhibitor."
4854483|"Studies on the disulfide bonds of glycoprotein hormones.
4904878|The disulfide bonds."
4919729|The assignment of the position of the six disulfide bridges."
4922544|"Interchain disulfide bridges of guinea pig gamma-2-immunoglobulin."
4923144|Intrachain disulfide bonds."
4940472|"Disulphide bridges of the heavy chain of human immunoglobulin G2."
4941626|"The disulfide bonds of viscotoxin A3 from the European mistletoe (Viscum album L., Loranthaceae)."
5073237|"The disulphide bridges of a mouse immunoglobulin G1 protein."
5135319|Determination of the disulfide bonds and proteolysis by thermolysin."
5166329|"The disulphide bonds of erabutoxin a, a neurotoxic protein of a sea-snake (Laticauda semifasciata) venom."
5296424|"The disulfide linkages in kallikrein inactivator of bovine lung."
5532232|"The disulfide bonds of bovine alpha-lactalbumin."
5533659|"The position of disulfide bonds in cobrotoxin."
5857373|"The disulfide bridges of hen's egg-white lysozyme."
5860161|The disulfide linkages."
5892911|"The disulphide bridges of trypsin."
5971783|"Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A."
6006643|"The amino acid sequences around the disulfide bonds of soybean trypsin inhibitor."
6162107|"Assignment of the disulphide bonds of leukocyte interferon."
6162107|The results indicate that Cys 1 is bonded to Cys 98, and Cys 29 is bonded to Cys 138.
6466616|"Conotoxin GI: disulfide bridges, synthesis, and preparation of iodinated derivatives."
6466616|Using this method, we show that the natural conotoxin GI has a (2-7, 3-13) disulfide configuration.
6526384|"The primary structure of human free secretory component and the arrangement of disulfide bonds."
6605967|"Disulfide bridges in an alpha-amylase inhibitor from wheat kernel."
6605967|The disulfide bond partners of residues 20 and 99 were not conclusively determined because of the difficulty of cleavage of the Cys-Cys bond at residues 41 and 42.
6630187|Disulfide bonding and conformational states."
6630187|In this work we have confirmed the primary structure and established the disulfide bonding configuration (Cys 3-Cys 8; Cys 4-Cys 14) by direct chemical synthesis of the toxin with specific disulfide bridges.
6723985|"A new assignment of the disulfide linkage in stellacyanin."
6723985|We infer that a disulfide switch occurs at higher pH and that in the native protein the disulfide bridge occurs between Cys-59 and Cys-93.
6768586|"The disulphide bonds of a Hong Kong influenza virus hemagglutinin."
6774759|"Studies on the disulfide bonds in human pituitary follicle-stimulating hormone."
6774759|The results indicate that the disulfide bonds are present between half-cystine residues located between positions 7 and 10, 28 and 87 and 82 and 84 in the alpha-subunit, and between positions 3 and 28, 17 and 51 and 32 and 104 in the beta-subunit of human FSH.
6860649|"Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation."
6860649|The two half-molecules are joined by three disulfide bonds, one between the two alpha-chains (residue alpha-28) and two between the two gamma-chains (residues gamma-8 and gamma-9).
6860649|A tryptic peptide containing gamma-chain residues 6-14 was isolated as a disulfide-linked dimer from CNBr-treated fragment E.
6884994|Within this region a so far not described additional intrapeptidal disulfide bridge could be localized (Cys 105-Cys 110) that creates a short loop with antiparallel running peptide strains in beta-pleated sheet conformation.
7151781|The disulfide bridges and the sulfhydryl groups."
7151781|Three bridges (Cys-4--Cys-10, Cys-237--Cys-261 and Cys-433--Cys-449) were easily identified in the peptic digest of lipase at pH 2.0.
7151781|In the latter digest, two other bridges (Cys-285--Cys-296 and Cys-299--Cys-304) were also identified by means of the cystine peptide constituted by two peptide segments: Ala281-Gly-Phe-Pro-Cys-Asp-Ser287 and Thr292-Ala-Asn-Lys-Cys-Phe-Pro-Cys-Pro-Ser-Glu-Gly-Cys-Pro-Gln-Met307.
7151781|Consequently it was concluded that Cys-285 is linked to Cys-296.
7151781|Therefore Cys-299 and Cys-304 are paired.
7151781|The results obtained for the characterization of the SHII group suggested the existence of two isomeric forms, the SHII being either on Cys-101 or Cys-103 and the bridge alternately between Cys-90--Cys-103 or Cys-90--Cys-101.
7151781|The bridge Cys-90--Cys-101 was characterized in a thermolytic digest of a cyanogen bromide fragment (CN II) of the protein.
7240231|"Assignment of disulfide bonds in the beta subunit of human chorionic gonadotropin."
7240231|From the specific radioactivities of S-[14C]carboxymethylcysteines in DS3.4-hCG-beta, four out of six disulfide bonds, 9-90, 26-110, 34-88, and 93-100 were assigned.
7240231|Similar data from DS1.4-hCG-beta gave the locations of the other two disulfide bonds, 23-72 and 38-57, while confirming the locations of four disulfide bonds derived from the radioactivity distribution in DS3.4-hCG-beta.
7240231|The results of controlled reduction and S-[14C]alkylation also indicate that disulfide bond 93-100 is the most reactive, followed by disulfide bond 26-110, and that the least reactive among all is 34-88.
7410363|Disulfide bonds of Cerebratulus lacteus toxin A-III."
7410363|Determination of the amino acid compositions of the purified peptides demonstrated the existence of disulfide bonds linking half-cystine residues 17 and 38, 23 and 34, and 48 and 61.
7410374|"Assignment of disulfide bonds in the alpha subunit of human chorionic gonadotropin."
7410374|Thus, all five disulfide bonds in hCG-alpha were assigned and are located at positions 7 and 31, 10 and 32, 28 and 60, 59 and 87, and 82 and 84.
7574684|"Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding."
7574684|Six disulfide linkages were determined to be Cys1-Cys7, Cys5-Cys14, Cys121-Cys145, Cys123-Cys163, Cys187-Cys235, and Cys271-Cys314, respectively.
7578102|"Disulfide bonds, N-glycosylation and transmembrane topology of skeletal muscle triadin."
7578102|This observation indicates that one of the intermolecular disulfide bonds is formed between the identical domains of two triadin molecules at cysteine 671.
7578102|Immunoblots performed with and without mercaptoethanol of the insoluble fragments using mAb AE8.91 indicate the presence of a dimer formed between identical domains of two triadin intermolecular disulfide linkage at cysteine 270.
7592821|Evidence for a yeast cell wall protein with multiple immunoglobulin-like domains with atypical disulfides."
7592821|Cys97 is disulfide-bonded to Cys114, forming an interdomain bond between domains I and II.
7592821|Cys202 is bonded to Cys300, in an atypical intradomain disulfide bond between the A and F strands of domain III.
7612619|"Participation of the disulfide bridge in the redox cycle of the ferredoxin from the hyperthermophile Pyrococcus furiosus: 1H nuclear magnetic resonance time resolution of the four redox states at ambient temperature."
7612619|These states differ in the redox state of the cluster, which is coordinated by Cys 11, Asp 14, Cys 17, and Cys 56, and of a disulfide bridge between Cys 21 and Cys 48.
7656012|"The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues."
7685339|"Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein."
7726578|The six disulfide bonds of bilineobin link Cys78 to Cys234, Cys120 to Cys188, Cys178 to Cys203, Cys7 to Cys141, Cys152 to Cys167, and Cys28 to Cys44.
7727365|This toxin has 66 amino acid residues and is stabilized by four disulfide bridges (Cys12-Cys65, Cys16-Cys41, Cys25-Cys46, and Cys29-Cys48).
7759498|"The ethylene response mediator ETR1 from Arabidopsis forms a disulfide-linked dimer."
7761426|"Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells."
7851440|"Structure, stability and biological properties of a N-terminally truncated form of recombinant human interleukin-6 containing a single disulfide bond."
7918355|The pattern of disulfide connectivity (4-19, 12-24, and 18-29) is the same as for the omega-conotoxins, which are Ca2+ channel ligands.
7918370|"Complete assignment of disulfide bonds in bovine dopamine beta-hydroxylase."
7918370|Edman sequencing of tryptic and peptic peptides determined linkages at positions Cys140-Cys582, Cys218-Cys269, Cys255-Cys281, Cys452-Cys474, Cys514-Cys514, and Cys516-Cys516, where cysteines at positions 514 and 516 on one monomer disulfide pair with their homologs on a second monomer.
7918370|Further analysis by LC/ESI/MS and MALDI/MS identified linkages at positions Cys376-Cys489 and Cys380-Cys551.
7918370|Cysteines 140 and 582 form a disulfide linkage that folds the C-terminus back in proximity to the N-terminus.
7918467|"Structure of human apolipoprotein D: locations of the intermolecular and intramolecular disulfide links."
7918467|Tryptic peptide analysis indicated that Cys41 and Cys16 are joined by a disulfide bridge.
7918467|Using a combination of manual Edman degradations and mass spectrometric analysis on a purified cluster of chymotryptic fragments, we identified an intramolecular disulfide bridge between Cys8 and Cys114 and an intermolecular bridge between Cys116 of apoD and Cys6 of apoA-II.
8013663|"The disulfide bridges of toxin 2 from the scorpion Centruroides noxius Hoffmann and its three-dimensional structure calculated using the coordinates of variant 3 from Centruroides sculpturatus."
8013663|They are: Cys12-Cys65, Cys16-Cys41, Cys25-Cys46 and Cys29-Cys48.
8056749|Among five half-cystine residues present in CLSI-III, two disulfide bonds link Cys44 to Cys88 and Cys142 to Cys149, Cys106 being present as a free cysteine residue.
8132555|"Mutational analysis of disulfide bridges in the type C atrial natriuretic peptide receptor."
8132555|An analysis of the mutant receptors expressed in COS-1 cells by 125I-ANP binding assay and by measuring difference in their electrophoretic mobilities on sodium dodecyl sulfate-polyacrylamide gels indicated that 1) the first 4 cysteine residues are joined sequentially, forming the Cys104-Cys132 and Cys209-Cys257 loops of 29 and 49 residues, respectively; 2) the two disulfide-linked loops are essential for the ligand binding activity; 3) the 5th cysteine residue Cys469 is used in the formation of covalently linked dimers; and 4) the covalent association of the subunit through the disulfide bond involving Cys469 has no apparent influence on ligand-receptor interactions.
8132555|The intramolecular disulfide bond Cys104-Cys132 was also confirmed by direct protein sequencing of tryptic fragments of purified ANP-C receptor.
8136023|"Assignment of the three disulfide bridges of huwentoxin-I, a neurotoxin from the spider selenocosmia huwena."
8136023|By sequencing disulfide cross-linked tryptic fragments, the three disulfide linkages in huwentoxin-I could be assigned as Cys2-Cys17, Cys9-Cys22, and Cys16-Cys29.
8137941|"Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein."
8137941|Of the 9 half-cystine residues, 5 are unpaired cysteines (Cys2, Cys23, Cys42, Cys64, and Cys96), while 4 form disulfides (Cys20-Cys115, and Cys92-Cys107).
8152378|"Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi."
8152378|The C-terminal cellulose-binding domain (CBD) of EGZ was found to contain a disulphide bond which forms, in the periplasm, between residues Cys-325 and Cys-382.
8179819|We have shown, in addition, that Cys-117 is involved in the formation of a disulfide-bonded homodimer of GRP94.
8180220|"Assignment of disulfide bond location in prothoracicotropic hormone of the silkworm, Bombyx mori: a homodimeric peptide."
8180220|The disulfide bond location of a homodimeric peptide, prothoracicotropic hormone (PTTH) of the silkworm, Bombyx mori, was determined by a combination of partial reduction and sequence analysis of peptide fragments generated through a partial reduction of PTTH followed by alkylation and enzyme digestion.
8180220|In conclusion, the disulfide bond location of PTTH was assigned to Cys15-Cys15' as an interchain disulfide linkage and Cys17-Cys54, Cys40-Cys96, and Cys48-Cys98 as intrachain disulfide linkages.
8181566|"Bovine seminal plasma aSFP: localization of disulfide bridges and detection of three different isoelectric forms."
8240271|"Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides."
8276756|"Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein."
8276756|The results indicated that disulfide bonds were formed at Cys3-Cys26, Cys6-Cys13, Cys19-Cys39, Cys45-Cys63 (or 64), and Cys63 (or 64)-Cys69.
8281941|The assignment of a disulfide bridge (Cys298-Cys303) was obtained by mass spectrometry.
8297371|The disulfide bridge pairing was similar to that found previously for the related toxin-charybdotoxin (3): from Cys7 to Cys29, from tested for inhibition of 125I margatoxin binding to voltage-activated potassium channels.
8307998|"Assignment of disulfide bonds in corticotropin-releasing factor-binding protein."
8348977|"Determination of the disulphide bridge arrangement of bovine histidine-rich glycoprotein."
8348977|Twelve half-cystine residues were found in bovine HRG (compared to sixteen cysteines in human HRG), all involved in the formation of six disulphide bridges connecting Cys-1 to Cys-12, Cys-2 to Cys-3, Cys-4 to Cys-5, Cys-6 to Cys-11, Cys-7 to Cys-8, and Cys-9 to Cys-10.
8355276|"Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data.
8364028|"Disulfide bond assignments and secondary structure analysis of human and murine interleukin 10."
8364028|The disulfide bond assignments for both species were similar in that the first cysteine residue in the sequence paired with the third and the second paired with the fourth.
8394346|"Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator.
8394346|The following disulfide bond structure was determined: Cys3-Cys24, Cys6-Cys12, Cys17-Cys45, and Cys71-Cys76.
8394346|However, an additional pair of cysteines present within these domains probably forms a fifth disulfide bond.
8399391|"Disulfide bridge structure of the heat-stable sweet protein mabinlin II."
8399391|The formation of two interchain disulfide bridges at Cys(A5)-Cys(B21) and Cys(A18)-Cys(B10), and two intrachain disulfide bridges at Cys(B11)-Cys(B59) and Cys(B23)-Cys(B67) were determined by amino-acid sequencing and composition analysis of cystine-containing peptides isolated by HPLC.
8405461|"Mass spectrometric evidence for a disulfide bond in aequorin regeneration."
8405461|The results showed that apoaequorin contains a disulfide bond between Cys145 and Cys152 and that the reduction of this bond is involved in the regeneration of aequorin.
8416818|"Disulfide bridges in human complement component C3b."
8416818|The 10 bridges are Cys537-Cys794, Cys605-Cys640, Cys851-Cys1491, Cys1079-Cys1136, Cys1336-Cys1467, Cys1367-Cys1436, Cys1484-Cys1489, Cys1496-Cys1568, Cys1515-Cys1639, and Cys1615-Cys1624.
8416818|Including the 3 bridges in C3a (Cys670-Cys698, Cys672-Cys705, and Cys685-Cys706) previously determined by high-resolution X-ray crystallography [Hoppe-Seyler's Z. Physiol. Chem. 361 (1980) 1389-1399] all disulfide bridges of C3 are localized.
8418848|"Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations."
8418848|The data show that the disulfide pairs are 4-19, 6-14, 13-36, 27-33, 32-57, and 45-64.
8422244|"The disulfide bond arrangement of leukemia inhibitory factor: homology to oncostatin M and structural implications."
8422244|The three disulfide bonds are CYS13-CYS135, CYS19-CYS132 and CYS61-164 and the first and third of these are clearly homologous to the two disulfide bonds in oncostatin M.
8422357|"Assignment of the inter- and intramolecular disulfide linkages in recombinant human macrophage colony stimulating factor using fast atom bombardment mass spectrometry."
8422357|The intermolecular disulfide bridges hold the dimer together and form symmetric bonds in which Cys31 and Cys157/Cys159 from one monomer unit are linked to the corresponding cysteines of the second monomer.
8422357|The intramolecular disulfide bonds are located between Cys7-Cys90, Cys48-Cys139, and Cys102-Cys146, respectively.
8430107|Seven disulfide bonds link half-cystine residues 2 to 13, 30 to 128, and 103 to 120 of the alpha subunit; 2 to 13, 30 to 121, and 98 to 113 of the beta subunit; and 80 of the alpha subunit to 75 of the beta subunit.
8443182|"Alignment of disulfide bonds of the extracellular domain of the interferon gamma receptor and investigation of their role in biological activity."
8443182|It was found that four consecutive disulfide bonds are formed between residues Cys60-Cys68, Cys105-Cys150, Cys178-Cys183, and Cys197-Cys218.
8443182|The specific antibodies gamma R38 and gamma R99 detected conformational epitopes stabilized by disulfide bonds involving cysteine residues 60 and 68, and 178 and 183, respectively.
8454636|"Characterization of the disulfide motif in BNBD-12, an antimicrobial beta-defensin peptide from bovine neutrophils."
8508052|"Determination of three disulfide bonds in a major house dust mite allergen, Der f II."
8508052|Determination of the amino acid sequence of each peptide collected in this way proved the existence of three disulfide bonds between Cys8 and Cys119, Cys21 and Cys27, and Cys73 and Cys78.
8508810|Disulfide bonds were detected between Cys21 and Cys21, Cys61 and Cys264, Cys194 and Cys198, and Cys296 and Cys351 in the amino acid sequence deduced from the cDNA.
8537186|"Determination of disulfide bridge pattern in omega-conopeptides."
8537186|All synthetic peptides, SNX-111, -157, -159, -183, -185, -230 and -231, were found to have the same disulfide bridge pattern as determined for the naturally occurring omega-conopeptide G-VI-A, i.e. disulfide bridges between the half-cystines 1-16, 8-20 and 15-25 (using the amino-acid numbering of SNX-111).
8624417|"Structural characterization and location of disulphide linkages of a potent vasodilatory peptide, recombinant maxadilan, by a multiple mass spectrometric approach."
8624417|Assignment of the Cys-5-Cys-9 linkage was achieved by comparison of FAB mass spectra before and after reduction of tryptic digests of r-maxadilan.
8624417|Since the molecular weight of the peptide fragment containing the Cys-18-Cys 55 linkage is more than 4000, MALDI measurement was indispensable for assignment of this linkage.
8670056|"The disulphide bond structure of thyroid-stimulating hormone beta-subunit."
8670056|The most reactive disulphide bond was Cys88-Cys95; the second most reactive group of disulphide bonds involved the half-cystine residues Cys16, Cys19, Cys67 and Cys105 with the experimental results consistent with the assignment of disulphide bonds to Cys16-Cys67 and Cys19-Cys105.
8670056|The isolation, by high-performance ion-exchange chromatography, of a partly reduced bTSH beta derivative in which only the half-cystine residues Cys31, Cys85, Cys88 and Cys95 were labelled enabled the assignment of a previously uncharacterized disulphide bond to Cys31-Cys85.
8670056|The remaining two assignments, Cys2-Cys52 and Cys27-Cys83, were made by comparison with the recently published human chorionic gonadotropin crystal structure.
8703941|"The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure."
8703941|Cys residues 188 and 201 in domain 2 of plasma gelsolin were disulfide linked.
8755737|"Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications."
8755737|Mass spectral analysis of cyanogen bromide peptides has established that the cystine connectivities follow a nearest-neighbor, aabbcc, pattern i.e., Cys152-Cys158, Cys352-Cys370, and Cys538-Cys550, in which the disulfides form three small loops of five, 17, and 11 residues, respectively.
8760356|Taken together, these results suggest that the alpha/beta heterodimeric form of meprin is held together by a single disulphide bond linking Cys309 in the alpha subunit to Cys306 in the beta subunit.
8770906|"A disulfide bonding interaction role for cysteines in the extracellular domain of the thyrotropin-releasing hormone receptor."
8770906|This study presents evidence that a disulfide bond exists between Cys98 and Cys179 which is essential for maintaining the receptor in the correct conformation for ligand binding.
8799123|"Agrobacterium tumefaciens VirB7 and VirB9 form a disulfide-linked protein complex."
8799123|Mutational studies demonstrate that cysteine residues at positions 24 of VirB7 and 262 of VirB9 participate in the formation of this complex.
8809084|"Carbonic anhydrase IV: purification of a secretory form of the recombinant human enzyme and identification of the positions and importance of its disulfide bonds."
8809084|Results indicated that the disulfide bonds in the native enzyme link Cys6 to Cys18 and Cys28 to Cys211.
8823187|Cys 361 alone is involved in disulfide-linked dimerization."
8823187|Thus, cysteine 361 is the only residue involved in disulfide linkage between the subunits.
8900177|Electron microscopic study of flexible, multidomain, fibrous proteins and determination of the disulfide bond pattern of the scavenger receptor cysteine-rich domain."
8900177|Proteolytic analysis was used to determine the intramolecular disulfide bonds in the type I-specific scavenger receptor cysteine-rich (SRCR) domain: Cys2-Cys7, Cys3-Cys8, and Cys5-Cys6.
8914841|"Positions of disulfide bonds in yam (Dioscorea japonica) acidic class IL (class IV) chitinase."
8914841|Four intradisulfide bonds containing peptides were purified and three disulfide bonds in the catalytic domain were identified as Cys-66 and Cys-115, Cys-128 and Cys-136, and Cys-218 and Cys-250.
8920961|"Analysis of the disulfide linkage pattern in circulin A and B, HIV-inhibitory macrocyclic peptides."
8920961|Thus, we were able to unambiguously identify the disulfide linkage pattern in circulin A and circulin B as Cys1-Cys4, Cys2-Cys5 and Cys3-Cys6, where the numbers on the cystine residues refer to their respective order in the peptides.
8988018|"Glial cell line-derived neurotrophic factor: selective reduction of the intermolecular disulfide linkage and characterization of its disulfide structure."
8988018|Under an acidic condition, the interchain disulfide bond was selectively cleaved with tris(2-carboxyethyl)phosphine, revealing that Cys101 was involved in the intermolecular disulfide linkage.
8988018|Three other disulfides, Cys68-Cys131, Cys72-Cys133, and Cys41-Cys102, were identified as intramolecular linkages.
9003812|"Functional consequences of disulfide bond formation in gelsolin."
9003812|Gelsolin is an actin monomer binding and filament severing protein synthesized in plasma and cytoplasmic forms differing by an N-terminal amino acid extension and a disulfide bond between Cys-188 and Cys-201.
9022673|"Chemical synthesis and characterization of maurotoxin, a short scorpion toxin with four disulfide bridges that acts on K+ channels."
9022673|The pairings were Cys3-Cys24, Cys9-Cys29, Cys13-Cys19 and Cys31-Cys34.
9030770|The six Cys residues of EPV20 were found to be disulfide-linked in a 1-6, 2-3 and 4 5 pattern.
9063464|Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity."
9063464|Disulfide bridges were assigned by peptide mapping on both natural and synthetic forms to be between Cys2-Cys37, Cys11-Cys30 and Cys20-Cys34.
9114491|It is stabilized by four disulfide bridges, formed between Cys12-Cys65, Cys16-Cys41, Cys25-Cys46 and Cys29-Cys48.
9126357|"The structure of synenkephalin (pro-enkephalin 1-73) is dictated by tree disulfide bridges."
9126357|Three disulfide bridges between Cys2-Cys24, Cys6-Cys28, and Cys9-Cys41 were identified.
9169621|"Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties."
9169621|alpha2AP is an exception from this generalization and has previously been shown to contain four Cys residues organized into two disulphide bridges [Lijnen, Holmes, van Hoef, Wiman, Rodriguez and Collen (1987) Eur. J. Biochem. 166, 565-574].
9169621|This observation prompted a re-examination of the state of the thiol groups, which revealed (i) a disulphide bridge between Cys43 and Cys116, (ii) that Cys76 is bound to a cysteinyl-glycine dipeptide, and (iii) and Cys125 exists as either a free thiol or in a mixed disulphide with another Cys residue.
9169621|The disulphide identified between Cys43 and Cys116 appears to be conserved in orthologous proteins since the homologous Cys residues form disulphide bonds in bovine and possibly mouse alpha2AP.
9176817|"Location of the three disulfide bonds in an antimicrobial peptide from Amaranthus caudatus using mass spectrometry."
9268356|"Biochemical characterization and mass spectrometric disulfide bond mapping of periplasmic alpha-amylase MalS of Escherichia coli."
9268356|The resulting peptides were separated by reverse phase-high performance liquid chromatography, and matrix-assisted laser desorption/ionization mass spectrometry analysis indicated the presence of two disulfide bonds, i.e. Cys40-58 and Cys104-520.
9268356|The disulfide bond at Cys40-58 is located in an N-terminal extension of about 160 amino acids which has no homology to other amylases but to the proposed peptide binding domain of GroEL, the Hsp60 of E. coli.
9268356|The N-terminal extension is linked to the C-terminal amylase domain via disulfide bond Cys104-520.
9359871|"A four-disulphide-bridged toxin, with high affinity towards voltage-gated K+ channels, isolated from Heterometrus spinnifer (Scorpionidae) venom."
9369214|"The disulphide bond pattern of bitistatin, a disintegrin isolated from the venom of the viper Bitis arietans."
9369214|Disulphide bonds between cysteines 16-34, 18-29, 28-51, 42-48, 47-72, and 60-79 are conserved in medium-long disintegrins flavoridin and kistrin (70 amino acids, 12 cysteines), and the two cysteine residues at positions 5 and 24 found in bitistatin but not in other disintegrin molecules are disulphide-bridged.
9407080|"Disulfide bond assignment in human interleukin-7 by matrix-assisted laser desorption/ionization mass spectroscopy and site-directed cysteine to serine mutational analysis."
9407080|Many of the anticipated hIL-7 tryptic fragments were detected including one with a molecular mass equivalent to the sum of two polypeptides linked through a disulfide bond formed from Cys residues (Cys3 and Cys142).
9407080|In contrast, a family of single disulfide bond-forming variants of hIL-7 were constructed by reintroducing Cys pairs (Cys3-Cys142, Cys35-Cys130, and Cys48-Cys93), and each could stimulate cell proliferation with an EC50 of 4 x 10(-9), 2 x 10(-8), and 2 x 10(-9) M, respectively.
9425062|"Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2."
9425062|The unpaired Cys residue residing on heavy chain 1, Cys26, appears to be modified by dihexosylation.
9425062|In heavy chain 1 the two disulfide bonds are formed between Cys210 and Cys213 and between Cys234 and Cys506, and in heavy chain 2, between Cys207 and Cys210 and between Cys596 and Cys597.
9430691|[14C]Iodoacetamide labeling of free thiols of cysteine residues in mutant connexin-43s showed that two pairs of intramolecular disulfide bonds are formed between Cys54 and Cys192 and between Cys187 and Cys198.
9468508|The intrachain disulfide bond pattern of domain V was established showing that these bonds are between cysteine pairs C1-C5, C2-C6, and C3-C4.
9497290|"Activation of the OxyR transcription factor by reversible disulfide bond formation."
9556602|"Disulfide bond structure of human epidermal growth factor receptor."
9556602|We identified a basic repeat of eight cysteines with a 1-3, 2-4, 5-6, and 7-8 disulfide pairing pattern in the two cysteine-rich regions of sEGFR.
9585534|The complete assignment of the disulfide bond revealed the involvement of cysteines 144 and 158 around copper-binding histidine residues.
9654146|The CART peptides contain six cysteine residues and using the yeast expressed CART(62-102) the disulphide bond configuration was found to be I-III, II-V and IV-VI.
9724530|"Determination of disulfide structure in agouti-related protein (AGRP) by stepwise reduction and alkylation."
9724530|The resulting proteins were characterized by peptide mapping, sequence analysis, and mass spectrometry, showing that AGRP contained a highly reducible disulfide bond, C85-C109, followed by less reactive ones, C90-C97, C74-C88, C67-C82, and C81-C99, respectively.
9786864|Determination of disulfide structure and N-glycosylation sites of the extracellular domain."
9792177|"Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels."
9792177|The half-cystine pairings of sMTX were determined by enzymatic cleavage and were found to be Cys3 Cys24, Cys9-Cys29, Cys13-Cys19, and Cys31-34, in agreement with experimental data obtained with natural maurotoxin.
9826197|"Assignment of disulfide bridges in bovine CD36."
9826197|We have found that there are no free cysteines in CD36 and that the six centrally clustered cysteines are linked by disulfide bonds, Cys242-Cys310, Cys271-Cys332 and Cys312-Cys321, resulting in a 1-3, 2-6 and 4-5 arrangement of the disulfide bridges.
9888818|Experiments with mutant proteins in which these three cysteine residues were replaced individually with serine suggest that Cys62-SH constitutes the site of oxidation by peroxides and that the oxidized Cys62 reacts with the Cys120-SH group of another type II TPx molecule to form an intermolecular disulfide linkage.
9917844|"A single disulfide bridge (Cys182-Cys264) is crucial for alpha-dystroglycan N-terminal domain stability."
9928020|The results indicate the existence of a disulfide bond between Cys215 and Cys285, which is important for stabilizing the receptor in the correct conformation for ligand binding and activation.
10026302|Three cystine pairs (Cys11-Cys25, Cys18-Cys29, and Cys24-Cys36) were determined by identification of the resulting peptides.
10026302|The disulfide pairings of the two adjacent Cys residues (Cys11-Cys25 and Cys24-Cys36) were unambiguously assigned by comparing the derived fragments with the two possible isomers synthesized through a novel disulfide-linking technique.
10066782|"Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor."
10066782|The disulfides Cys102-Cys113 and Cys146-Cys157 are consistent with known cytokine-binding domain motifs, and Cys28-Cys77 with known Ig superfamily domains.
10066782|An unusual cysteine connectivity between Cys6-Cys174, which links the Ig-like and NH2-terminal FN III domains causing them to fold back onto each other, has not previously been observed among cytokine receptors.
10080355|The positions of four disulfide bridges in BmK AS-1 were established as Cys-12 and Cys-62, Cys-16 and Cys-37, Cys-23 and Cys-44, and Cys-27 and Cys-46, which are the same as those in alpha- and beta-scorpion neurotoxins.
10198206|"Assignment of disulfide linkages in chum salmon stanniocalcin."
10198206|Chum salmon STC is a homodimer connected by a single intermonomeric disulfide bond at Cys169.
10198206|The monomer consists of 179 amino-acids, containing five intramonomeric disulfide bonds formed between Cys12-Cys26, Cys21-Cys41, Cys32-Cys81, Cys65-Cys95, and Cys102-Cys137.
10214721|The technique permitted not only the reading frame of this enzyme, the amino acid sequence of which was deduced from DNA, but also the elucidation of an N-terminal blocking group and the position of a disulfide bridge between Cys309 and Cys365 among the three Cys residues.
10214721|A free cysteine (Cys127) was identified by modifying an intact molecule with a sulfhydryl reagent, 5-(octyldithio)-2-nitrobenzoic acid, under non-reducing conditions.
10329650|"The N-terminal disulfide linkages of human insulin-like growth factor-binding protein-6 (hIGFBP-6) and hIGFBP-1 are different as determined by mass spectrometry."
10329650|Numbering IGFBP-6 cysteines sequentially from the N terminus, the first three disulfide linkages are Cys1-Cys2, Cys3-Cys4, and Cys5-Cys6.
10329650|The next two linkages are Cys7-Cys9 and Cys8-Cys10, which are analogous to those previously determined for IGFBP-3 and IGFBP-5.
10329650|The C-terminal linkages are Cys11-Cys12, Cys13-Cys14, and Cys15-Cys16, analogous to those previously determined for IGFBP-2.
10329650|Analogous with IGFBP-3, IGFBP-5, and IGFBP-6, Cys9-Cys11 and Cys10-Cys12 of IGFBP-1 are also disulfide-linked.
10333293|Bactericidal/permeability-increasing protein, which is a member of the same gene family, contains an essential disulfide bond between Cys135 and Cys175; these residues, which correspond to Cys129 and Cys168 in PLTP, are conserved among all known members of the gene family.
10366732|"Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori."
10366732|In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis.
10366732|Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide bond.
10406958|It was found that the main form of saposin D consists of 80 amino acid residues and that the six cysteine residues are linked in the following order: Cys5-Cys78, Cys8-Cys72 and Cys36-Cys47.
10449041|"The disulfide bond arrangement in the extracellular domain of the activin type II receptor."
10449041|By combining proteolysis with mass spectroscopy and chemical sequence analysis, the disulfide connectivity was determined to be as follows: C1-C3, C2-C4, C5-C8, C6-C7, and C9-C10.
10473547|"Sequence, S-S bridges, and spectra of bovine transcobalamin expressed in Pichia pastoris."
10473547|Three S-S bonds connected Cys residues 3-252, 98-294, and 147-190.
10527498|Furthermore, a disulfide bridge between Cys17 and Cys38 was ascertained.
10600112|Cleavage is followed by the reduction of a key disulfide bond (cysteines 265-287).
10600112|These data indicate that PE reduction is a two-step process: unfolding that allows access to the Cys265-287 disulfide bond, followed by reduction of the sulfur-sulfur bond by PDI or a PDI-like enzyme.
10600112|With regard to cellular processing, we propose that the toxin's three-dimensional structure retains a "closed" conformation that restricts solvent access to the Cys265-287 disulfide bond until after a cell-mediated unfolding event.
10601859|"Assignment of a single disulfide bridge in rat liver methionine adenosyltransferase."
10601859|The results obtained revealed a disulfide bridge between Cys35 and Cys61.
10642516|"Disulphide-bond pattern and molecular modelling of the dimeric disintegrin EMF-10, a potent and selective integrin alpha5beta1 antagonist from Eristocophis macmahoni venom."
10664838|Prediction of the secondary structure and identification of intramolecular disulfide bridges."
10664838|Eight peptides, which constitute three sets of cystine-containing peptides, were purified by HPLC from a thermolytic digest of RA17 and identified by their amino acid sequence and composition, indicating five intramolecular disulfide bridges: Cys34-Cys94, Cys26-(Cys50 or Cys51)-Cys110 and Cys12-(Cys62 or Cys64)-Cys122.
10667857|"Assignment of the disulfide bonds of Ole e 1, a major allergen of olive tree pollen involved in fertilization."
10667857|Specific proteolysis with thermolysin and reverse-phase HPLC separation of the peptides allowed the determination of the disulfide bond between Cys43 and Cys78.
10667857|Amino acid compositions and Edman degradation of the peptide products indicated the presence of the disulfide bonds at Cys19-Cys90 and Cys22-Cys131.
10764757|"Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone."
10764757|Matrix-assisted laser desorption/ionization-mass spectrometry peptide mapping in combination with in vitro and on target protein chemical modification showed that this activation process of Hsp33 is accompanied by the formation of two intramolecular disulfide bonds within Hsp33: Cys(232)-S-S-Cys(234) and Cys(265)-S-S-Cys(268).
10833271|The enzyme consists of a single polypeptide chain of 177 amino acid residues with one disulfide bond, Cys114-Cys121.
10880981|"Kiwi protein inhibitor of pectin methylesterase amino-acid sequence and structural importance of two disulfide bridges."
10880981|Analysis of fragments obtained after digestion of the protein alkylated without previous reduction identified two disulfide bridges connecting Cys9 with Cys18, and Cys74 with Cys114; Cys140 bears a free thiol group.
10913300|"The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern."
10913300|Analysis of the disulfide bond pattern of the refolded receptor fragment revealed disulfide bonds between Cys170 and Cys131, Cys148 and Cys108, and Cys117 and Cys48.
10926678|This led to the identification of one disulfide bridge between C306 and C334; reconsideration of the topological model predictions suggested a second disulfide bridge between C225 and C520.
10926678|Evaluation of a fourth double mutant indicated that at least one of two disulfide bridges (C306 and C334; C225 and C520) has to be formed to allow the surface expression of a functional cotransporter.
10926678|A revised secondary structure is proposed which includes two partially repeated motifs that are connected by disulfide bridges formed between cysteine pairs C306-C334 and C225-C520.
10945991|Taken together, the results suggest that Cys-140 contributes to intermolecular disulfide-linked dimerization of mGluR1.
10956019|Contortrixobin (i) has six disulfide bonds whose sequence positions have been determined by mass spectrometry and (ii) does not contain carbohydrates in its structure.
10970898|Toward new insights in the understanding of their distinct disulfide bridge patterns."
10970898|It is a 34-residue peptide cross-linked by four disulfide bridges that are in an "uncommon" arrangement of the type C1-C5, C2-C6, C3-C4, and C7-C8 (versus C1-C5, C2-C6, C3-C7, and C4-C8 for Pi1 or HsTx1, two MTX-related scorpion toxins).
11018043|"Disulfide bonds of GM2 synthase homodimers.
11018043|All Cys residues of the lumenal domain of GM2 synthase are disulfide bonded with Cys(429) and Cys(476) forming a disulfide-bonded pair while Cys(80) and Cys(82) are disulfide bonded in combination with Cys(412) and Cys(529).
11018043|Partial reduction to produce monomers converted Cys(80) and Cys(82) to free thiols while the Cys(429) to Cys(476) disulfide remained intact.
11018043|In summary these results demonstrate that Cys(429) and Cys(476) form an intrasubunit disulfide while the intersubunit disulfides formed by both Cys(80) and Cys(82) with Cys(412) and Cys(529) are responsible for formation of the homodimer.
11031261|These peptides, which we have named as Tigerinins, are characterized by an intramolecular disulfide bridge between two cysteine residues forming a nonapeptide ring.
11063595|Dpl 24-152 was shown to contain two disulfide bonds (Cys94-Cys145 and Cys108-Cys140).
11080501|"Determination of disulfide bond assignments and N-glycosylation sites of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM)."
11080501|Numbering GA733-2 cysteines sequentially from the N terminus, the first three disulfide linkages are Cys1-Cys4, Cys2-Cys6, and Cys3-Cys5, which is a novel pattern for a cysteine-rich domain instead of the expected epidermal growth factor-like disulfide structure.
11080501|The next three disulfide linkages are Cys7-Cys8, Cys9-Cys10, and Cys11-Cys12, consistent with the recently determined disulfide pattern of the thyroglobulin type 1A domain of insulin-like growth factor-binding proteins 1 and 6.
11098061|"Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130."
11098061|The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061|Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061|An eight-residue loop in domain 5 is tethered by Cys(436)-Cys(444).
11099505|This peptide was purified to homogeneity using reversed-phase high performance liquid chromatography and found to have the following primary structure by Edman degradation and pyridylethylation: LVRGCWTKSYPPKPCFVR, in which Cys(5) and Cys(15) are disulfide bridged.
11133953|"Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase."
11133953|The lipase contains two cysteine residues which form an intramolecular disulfide bond.
11182766|"Expression, purification and characterization of the structure and disulfide linkages of insulin-like growth factor binding protein-4."
11182766|The established linkages were C3 to C8, C4 to C7, C9 to C 11, and C10 to C12.
11182766|The two cysteines in the non-conserved mid-region unique to IGFBP-4 (C13 and C14) are linked together.
11182766|Linkage of the C-terminal cysteine residues is identical to that of IGFBP-2, -5 and -6 (C15 to C16, C17 to C18 and C19 to C20).
11209756|Both species of PSPI-21 are composed of two chains, named chains A and B, which are linked by a disulfide bridge between Cys(146) and Cys(157).
11209756|The other disulfide bridge is located within the A chains between Cys(48) and Cys(97).
11278697|"Conserved cysteines in the sialyltransferase sialylmotifs form an essential disulfide bond."
11279095|"Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity."
11283002|Further experiments showed that Cys(66) and Cys(63), which are located in the tolloid-specific sequence Cys(63)-Gly(64)-Cys(65)-Cys(66) in the active site, most likely form a disulfide bridge.
11369866|"Disulfide structure of alfimeprase: A recombinant analog of fibrolase."
11369866|The three disulfide bonds were determined to be Cys-116/196, Cys-156 /180, and Cys-158/163 with the residue number system of alfimeprase.
11425803|"Neighboring cysteine residues in human fucosyltransferase VII are engaged in disulfide bridges, forming small loop structures."
11425803|The results demonstrated that Cys(68)-Cys(76), Cys(211)-Cys(214), and Cys(318)-Cys(321) are disulfide-linked.
11454874|"Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains."
11454874|Conservation of Cys residues among CD47 homologues suggested the existence of a disulfide bond between the Ig and MMS domains that was confirmed by chemical digestion and mapped to Cys(33) and Cys(263).
11501762|"Assignment of the complete disulphide bridge pattern in the human recombinant follitropin beta-chain."
11501762|The pattern of cysteine couplings in betaFSH was determined as: Cys3-Cys5l, Cys17-Cys66, Cys20-Cys104, Cys28-Cys82, Cys32-Cys84 and Cys87-Cys94, confirming the arrangement inferred from the crystal structure of the homologous betaCG.
11501762|A subset of the S-S bridge pattern comprising Cys3-Cys51, Cys28-Cys82 and Cys32-Cys84 constitutes a cysteine knot motif similar to that found in the growth factor superfamily.
11567096|With protein fragmentation, Edman degradation, and mass spectrometric analysis, evidence was found for the signal peptide cleavage site C-terminally to Thr(23) and three disulfide bridges between precursor residues 30 and 54, 44 and 87, and 68 and 102.
11590138|"Disulfide connectivity of recombinant C-terminal region of human thrombospondin 2."
11590138|Mass spectrometry of the recombinant proteins digested with endoproteinase Asp-N revealed that disulfide pairing of the 18 cysteines in the Ca(2+)-binding repeats and C-terminal sequence is sequential, i.e. a 1-2, 3-4, 5-6, etc., pattern.
11693532|"CSTX-9, a toxic peptide from the spider Cupiennius salei: amino acid sequence, disulphide bridge pattern and comparison with other spider toxins containing the cystine knot structure."
11693532|The four disulphide bonds present in CSTX-9 are arranged in the following pattern: 1-4, 2-5, 3-8 and 6-7 (Cys6-Cys21, Cys13-Cys30, Cys20-Cys48, Cys32-Cys46).
11732689|"Assignment of the disulfide bridges in bothropstoxin-I, a myonecrotic Lys49 PLA2 homolog from Bothrops jararacussu snake venom."
11732689|Following this procedure, four bridges were initially identified from the tryptic and SV8 digests: Cys5O-Cysl31, Cys51-Cys98, Cys61-Cys91, and Cys84-Cys96.
11732689|From the chymotryptic digest other peptides were isolated either containing some of the above bridges, therefore confirming the results from the tryptic digest, or presenting a new bond between Cys27 and Cys123.
11732689|The two remaining bridges were identified as Cys29-Cys45 and Cys44-Cys105 by determination of the crystal structure, showing that BthTX-I disulfide bonds follow the normal pattern of group II PLA2s.
11749971|We show that Cys2 and Cys61 are covalently linked and that residue Cys155 bears the free sulfhydryl group.
11809854|"Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface."
11809854|Based on phenotypic comparisons of single and double cysteine mutants, we propose the following disulfide bond pairs in the human P2X(1) receptor: C117-C165, C126-C149, C132-C159, C217-C227, and C261-C270.
11809854|However, trafficking of the receptor to the cell membrane is severely reduced by disruption of the C261-C270 disulfide bond or disruption of C117-C165 together with another bond.
11856755|"Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat."
11856755|The dimer was linked by a disulfide through Cys(9) pairing.
11863449|"A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond."
11937510|By substituting each PLAP Cys by Ser, we found that disrupting the disulfide bond between Cys-121 and Cys-183 completely prevents the formation of the active enzyme, whereas the carboxyl-terminally located Cys-467-Cys-474 bond plays a lesser structural role.
11953458|"The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity."
11953458|We investigated variants of BACE in which the disulphide bonds of the catalytic domain spanning between Cys216/Cys420, Cys278/Cys443 and Cys330/Cys380 were removed by mutagenesis.
11953458|For the generation of a functional enzyme the conserved Cys330/Cys380 bond was the most critical, whereas the two bonds between Cys216/Cys420 and Cys278/Cys443, which are typical for the membrane-bound BACE, appeared to be less important.
12009896|"Identification of human vesicle monoamine transporter (VMAT2) lumenal cysteines that form an intramolecular disulfide bond."
12009896|The identity of the disulfide-bound cysteine pair was suggested by the observation that replacement of Cys 126 or Cys 333 with serine both reduced [(3)H]serotonin transport.
12009896|We conclude that human VMAT2 Cys 126 in loop 1/2 and Cys 333 in loop 7/8 form a disulfide bond which contributes to efficient monoamine transport.
12019263|"Identification of the disulfide bonds in the recombinant somatomedin B domain of human vitronectin."
12019263|Two pairs of disulfide bonds at the NH(2)-terminal portion of active rSMB were identified as Cys(5)-Cys(9) and Cys(19)-Cys(21).
12019263|The other two pairs of disulfide bonds in the COOH-terminal portion of rSMB were identified as Cys(25)-Cys(31) and Cys(32)-Cys(39) by protease-generated peptide mapping of partially reduced and S-alkylated rSMB.
12067732|"Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv."
12067732|The primary structurs all contain 10 cysteines, which are cross-linked to form five disulfide bridges with a pairing pattern (C1-C5, C2-C9, C3-C6, C4-C7, C8-C10).
12421832|Disulfide structure and carbohydrate attachment."
12450399|"Biophysical characterization, including disulfide bond assignments, of the anti-angiogenic type 1 domains of human thrombospondin-1."
12450399|By a combination of proteolysis and mass spectrometry, the recombinant TSRs were determined to be fully disulfide bonded with a connectivity of 1-5, 2-6, and 3-4 (cysteines are numbered sequentially from N- to C-terminus).
12475222|The cystine bridge connectivity of ProTx-II is very similar to that of other members of this family, i.e., C(2) to C(16), C(9) to C(21), and C(15) to C(25).
12493837|We identified several circulating forms of LEAP-2 differing in their amino-terminal length, all containing a core structure with two disulfide bonds formed by cysteine residues in relative 1-3 and 2-4 positions.
12615070|The olfactomedin-domain contains a single disulphide-bond connecting Cys-245 and Cys-433 residues; secondary structure predictions and circular dichroism studies indicate that it consists primarily of beta-strands.
12631268|MALDI-MS analysis of the resulting peptides revealed the four disulfide bonds Cys120-Cys131, Cys385-Cys431, Cys584-Cys588 and Cys594-Cys607.
12631268|Two additional disulfide bonds (Cys221-Cys226 and Cys227-Cys250) which were not directly accessible by tryptic cleavage, were identified by a combination of a method of partial reduction and MALDI-PSD analysis.
12631268|In the sphingolipid activator protein (SAP)-homologous N-terminal domain of haSMase, one disulfide bond was assigned as Cys120-Cys131.
12642668|"The role of disulfide bonds in the assembly and function of MD-2."
12642668|Structural analyses revealed that C95 and C105 formed an intrachain disulfide bond, whereas C95 by itself produced an inactive dimer.
12827284|The amino acid sequence was determined by Edman degradation, revealing it to be a 35-residue polypeptide amidated at its C terminal and including three disulfide bridges: Cys2-Cys17, Cys9-Cys24, and Cys16-Cys31 assigned by partial reduction and sequence analysis.
12919325|These studies showed that Cys115 forms a disulfide bond with Cys133, Cys128 with Cys149, and Cys131 with Cys140.
12921863|"Intracellular disulfide bond that affects ATP responsiveness of P2X(2) receptor/channel."