Distribution of amino acids in functional sites of proteins with high melting temperature.

ABSTRACT: The stability of proteins in its native state has an important implication on its function and evolution. The functional site analysis may lead to better understanding of how these amino acid distributions influence the melting temperature of proteins. It has been reported that increasing the fraction of hydrophobic contacts in a protein tends to raise melting temperature; increasing the fraction of repulsive charge contacts decrease the melting temperature and consistent with a destabilizing effect. The role of amino acid distribution as hydrophobic, charged and polar residues in proteins and mainly in its functional sites has been studied. Due to limited data availability, redundancy check and controlled environment parameters, the study was carried out with ten single chain-wild protein

SUBMITTER: Maheshwari AS 

PROVIDER: S-EPMC3530888 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature