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Conformations of disulfide bridges in proteins

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

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Official URL: http://www3.interscience.wiley.com/journal/1216351...

Abstract

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 Cβ 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: Journal Article
Additional Information: Copyright of this article belongs to John Wiley & Sons.
Keywords: cystine residues -disulfide bonds -disulfide conformation - protein conformation -protein data analysis
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: Ms TV Yashodha
Date Deposited: 03 Jun 2010 09:45
Last Modified: 22 Sep 2010 04:54
URI: http://eprints.iisc.ac.in/id/eprint/27235

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