Four distances between pairs of amino acids provide a precise description of their interaction.

ABSTRACT: The three-dimensional structures of proteins are stabilized by the interactions between amino acid residues. Here we report a method where four distances are calculated between any two side chains to provide an exact spatial definition of their bonds. The data were binned into a four-dimensional grid and compared to a random model, from which the preference for specific four-distances was calculated. A clear relation between the quality of the experimental data and the tightness of the distance distribution was observed, with crystal structure data providing far tighter distance distributions than NMR data. Since the four-distance data have higher information content than classical bond descriptions, we were able to identify many unique inter-residue features not found previously in protei

SUBMITTER: Cohen M 

PROVIDER: S-EPMC2715887 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature