Thermodynamic stability of histone H3 is a necessary but not sufficient driving force for its evolutionary conservation.

ABSTRACT: Determining the forces that conserve amino acid positions in proteins across species is a fundamental pursuit of molecular evolution. Evolutionary conservation is driven by either a protein's function or its thermodynamic stability. Highly conserved histone proteins offer a platform to evaluate these driving forces. While the conservation of histone H3 and H4 "tail" domains and surface residues are driven by functional importance, the driving force behind the conservation of buried histone residues has not been examined. Using a computational approach, we determined the thermodynamically preferred amino acids at each buried position in H3 and H4. In agreement with what is normally observed in proteins, we find a significant correlation between thermodynamic stability and evolutionary conse

SUBMITTER: Ramachandran S 

PROVIDER: S-EPMC3017104 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature