Analysis on conservation of disulphide bonds and their structural features in homologous protein domain families.

ABSTRACT:

Background

Disulphide bridges are well known to play key roles in stability, folding and functions of proteins. Introduction or deletion of disulphides by site-directed mutagenesis have produced varying effects on stability and folding depending upon the protein and location of disulphide in the 3-D structure. Given the lack of complete understanding it is worthwhile to learn from an analysis of extent of conservation of disulphides in homologous proteins. We have also addressed the question of what structural interactions replaces a disulphide in a homologue in another homologue.

Results

Using a dataset involving 34,752 pairwise comparisons of homologous protein domains corresponding to 300 protein domain families of known 3-D structures, we provide a comprehensive analysis

SUBMITTER: Thangudu RR 

PROVIDER: S-EPMC2628669 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature