A hydrophobic spine stabilizes a surface-exposed α-helix according to analysis of the solvent-accessible surface area.

ABSTRACT:

Background

Most of hydrophilic and hydrophobic residues are thought to be exposed and buried in proteins, respectively. In contrast to the majority of the existing studies on protein folding characteristics using protein structures, in this study, our aim was to design predictors for estimating relative solvent accessibility (RSA) of amino acid residues to discover protein folding characteristics from sequences.

Methods

The proposed 20 real-value RSA predictors were designed on the basis of the support vector regression method with a set of informative physicochemical properties (PCPs) obtained by means of an optimal feature selection algorithm. Then, molecular dynamics simulations were performed for validating the knowledge discovered by analysis of the selected PCPs.

Re

SUBMITTER: Liou YF 

PROVIDER: S-EPMC5259910 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature