Conformations of disulfide bridges in proteins

Srinivasan, N. ; Sowdhamini, R. ; Ramakrishnan, C. ; Balaram, P. (1990) Conformations of disulfide bridges in proteins International Journal of Peptide and Protein Research, 36 (2). pp. 147-155. ISSN 0367-8377

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The conformational characteristics of disulfide bridges in proteins have been analyzed using a dataset of 22 protein structures, available at a resolution of ≤ 2.0 Å, containing a total of 72 disulfide crosslinks. The parameters used in the analysis include (φ, ψ) values at Cys residues, bridge dihedral angles χss, χ1i, χ1j, χ2i and χ2j the distances Cαi-Cαj and Cβi-Cβj between the Cα and β atoms of Cys(i) and Cys(j). Eight families of bridge conformations with three or more occurrences have been identified on the basis of these stereochemical parameters. The most populated family corresponds to the "left handed spiral" identified earlier by Richardson ((1981) Adv. Protein Chem. 34, 167-330). Disulfide bridging across antiparallel extended strands is observed in α-lytic protease, crambin, and β-trypsin and this structure is shown to be very similar to those obtained in small cystine peptides. Solvent accessible surface area calculations show that the overwhelming majority of disulfide bridges are inaccessible to solvent.

Item Type:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
Keywords:Cystine Residues; Disulfide Bonds; Disulfide Conformation; Protein Conformation; Protein Data Analysis
ID Code:4117
Deposited On:13 Oct 2010 06:45
Last Modified:16 May 2011 06:48

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