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



Amutha Selvaraj Maheshwari1, 2 & Govindaraju Archunan1*



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; *Corresponding author


Article Type



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 80C 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.



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



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

Edited by

P Kangueane






Biomedical Informatics



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.