Quantitative theory of hydrophobic effect as a driving force of protein structure.

ABSTRACT: Various studies suggest that the hydrophobic effect plays a major role in driving the folding of proteins. In the past, however, it has been challenging to translate this understanding into a predictive, quantitative theory of how the full pattern of sequence hydrophobicity in a protein shapes functionally important features of its tertiary structure. Here, we extend and apply such a phenomenological theory of the sequence-structure relationship in globular protein domains, which had previously been applied to the study of allosteric motion. In an effort to optimize parameters for the model, we first analyze the patterns of backbone burial found in single-domain crystal structures, and discover that classic hydrophobicity scales derived from bulk physicochemical properties of amino acids a

SUBMITTER: Perunov N 

PROVIDER: S-EPMC3970890 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature