Prediction and analysis of surface hydrophobic residues in tertiary structure of proteins.

ABSTRACT: The analysis of protein structures provides plenty of information about the factors governing the folding and stability of proteins, the preferred amino acids in the protein environment, the location of the residues in the interior/surface of a protein and so forth. In general, hydrophobic residues such as Val, Leu, Ile, Phe, and Met tend to be buried in the interior and polar side chains exposed to solvent. The present work depends on sequence as well as structural information of the protein and aims to understand nature of hydrophobic residues on the protein surfaces. It is based on the nonredundant data set of 218 monomeric proteins. Solvent accessibility of each protein was determined using NACCESS software and then obtained the homologous sequences to understand how well solvent expos

SUBMITTER: Malleshappa Gowder S 

PROVIDER: S-EPMC3930195 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature