Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation(921 views) De Simone A, Berisio R, Zagari A, Vitagliano L
Keywords: Data Mining, Disulfide Bridges, Protein And Peptide Structure, Protein Data Bank, Statistics, Amino Acid, Cysteine, Polypeptide, Alpha Chain, Alpha Helix, Amino Acid Sequence, Article, Beta Chain, Disulfide Bond, Information Processing, Priority Journal, Protein Analysis, Protein Database, Protein Determination, Protein Folding, Protein Localization, Protein Motif, Protein Secondary Structure, Protein Stability, Protein Synthesis, Structural Proteomics, Protein Structure,
Affiliations: *** IBB - CNR ***
Dipartimento delle Scienze Biologiche, Sezione Biostrutture, Università degli Studi di Napoli Federico II, I-80134 Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), I-80134 Napoli, Italy
References: Not available.
Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation
Disulfide bridges have an enormous impact on the structure of a large number of proteins and polypeptides. Understanding the structural basis that regulates their formation may be important for the design of novel peptide-based molecules with a specific fold and stability. Here we report a statistical analysis of the relationships between secondary structure and disulfide bond formation, carried out using a large database of protein structures. Our analyses confirm the observation sporadically reported in previous investigations that cysteine residues located in a-helices display a limited tendency to form disulfide bridges. The very low occurrence of the disulfide bond in all a-chains compared to all beta-chains indicates that this property is also evident when proteins with different topologies are investigated. Taking advantage of the large database that endorsed the analysis on relatively rare motifs, we demonstrate that cysteine residues embedded in 3 (10) helices present a good tendency to form disulfide bonds. This result is somewhat surprising since 3 (10) helices are commonly assimilated into a-helices. A plausible structural explanation for the observed data has been derived combining analyses of disulfide bond sequence separation and of the length of the different secondary structure elements. Copyright (c) 2006 European Peptide Society and John Wiley & Sons, Ltd
Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation
Kim YH, Shin SW, Pellicano R, Fagoonee S, Choi IJ, Kim YI, Park B, Choi JM, Kim SG, Choi J, Park JY, Oh S, Yang HJ, Lim JH, Im JP, Kim JS, Jung HC, Ponzetto A, Figura N, Malfertheiner P, Choi IJ, Kook MC, Kim YI, Cho SJ, Lee JY, Kim CG, Park B, Nam BH, Bae SE, Choi KD, Choe J, Kim SO, Na HK, Choi JY, Ahn JY, Jung KW, Lee J, Kim DH, Chang HS, Song HJ, Lee GH, Jung HY, Seta T, Takahashi Y, Noguchi Y, Shikata S, Sakai T, Sakai K, Yamashita Y, Nakayama T, Leja M, Park JY, Murillo R, Liepniece-karele I, Isajevs S, Kikuste I, Rudzite D, Krike P, Parshutin S, Polaka I, Kirsners A, Santare D, Folkmanis V, Daugule I, Plummer M, Herrero R, Tsukamoto T, Nakagawa M, Kiriyama Y, Toyoda T, Cao X, Corral JE, Mera R, Dye CW, Morgan DR, Lee YC, Lin JT, Garcia Martin R, Matia Cubillo A, Lee SH, Park JM, Han YM, Ko WJ, Hahm KB, Leontiadis GI, Ford AC, Ichinose M, Sugano K, Jeong M, Park JM, Han YM, Park KY, Lee DH, Yoo JH, Cho JY, Hahm KB, Bang CS, Baik GH, Shin IS, Kim JB, Suk KT, Yoon JH, Kim YS, Kim DJ * Helicobacter pylori Eradication for Prevention of Metachronous Recurrence after Endoscopic Resection of Early Gastric Cancer(1203 views) N Engl J Med (ISSN: 0028-4793, 0028-4793linking, 1533-4406electronic), 2015 Jun; 30642104201566393291: 749-756. Impact Factor:59.558 ViewExport to BibTeXExport to EndNote