Title

Authors

Affiliation

¹Department of Animal Science, School of Life Sciences, Bharathidasan University, Tiruchirappalli – 620 024, Tamil Nadu, India; ²Department of Biotechnology, Anna University – BIT campus, Tiruchirappalli – 620 024, Tamil Nadu, India

Email

archunan@bdu.ac.in; *Corresponding author

Article Type

Hypothesis

Date

Received September 27, 2012; Accepted October 26, 2012; Published November 23, 2012

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 proteins having melting temperature above 80°C at pH 7. The analysis depicts that, the entire protein, hydrophobic residues are more frequent in single chain proteins and charged residues are more frequent in multi-chains proteins. In functional sites of these proteins, hydrophobic and charged residues are equally frequent in single chain proteins and charged residues are very high in multi-chains proteins. But, the polar residue distribution remains same for both single chain and multi-chain proteins and its functional sites.

Keywords

Classified amino acids, Functional residues, Melting temperature, Single and Multi-chain, Thermo-stable proteins.

Citation

Maheshwari & Archunan, Bioinformation 8(23): 1176-1181 (2012)
 

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.