Inter-residue distances derived from fold contact propensities correlate with evolutionary substitution costs.

ABSTRACT:

Background

The wealth of information on protein structure has led to a variety of statistical analyses of the role played by individual amino acid types in the protein fold. In particular, the contact propensities between the various amino acids can be converted into folding energies that have proved useful in structure prediction. The present study addresses the relationship of protein folding propensities to the evolutionary relationship between residues.

Results

The contact preferences of residue types observed in a representative sample of protein structures are converted into a residue similarity matrix or inter-residue distance matrix. Remarkably, these distances correlate excellently with evolutionary substitution costs. Residue vectors are derived from the distance m

SUBMITTER: Williams G 

PROVIDER: S-EPMC526251 | biostudies-literature | 2004 Oct

REPOSITORIES: biostudies-literature