Structural insights into the evolution of a non-biological protein: importance of surface residues in protein fold optimization.

ABSTRACT: Phylogenetic profiling of amino acid substitution patterns in proteins has led many to conclude that most structural information is carried by interior core residues that are solvent inaccessible. This conclusion is based on the observation that buried residues generally tolerate only conserved sequence changes, while surface residues allow more diverse chemical substitutions. This notion is now changing as it has become apparent that both core and surface residues play important roles in protein folding and stability. Unfortunately, the ability to identify specific mutations that will lead to enhanced stability remains a challenging problem. Here we discuss two mutations that emerged from an in vitro selection experiment designed to improve the folding stability of a non-biological ATP bi

SUBMITTER: Smith MD 

PROVIDER: S-EPMC1867856 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature