1 Department of Biotechnology, Periyar Maniammai University, Thanjavur – 613403, Tamil Nadu, India.
2 PG Department of Biotechnology and Bioinformatics, Bishop Heber College, Tiruchirappalli-17, Tamilnadu, India.
3 Department of Bioinformatics, Ponnaiyah Ramajayam College, Thanjavur – 614904, Tamil Nadu, India.
4 Department of Bioinformatics, Marudu Pandiyar College, Thanjavur – 620024, Tamil Nadu, India.
* Corresponding author
Proteins prefer to have 31.44% of carbon and 27% of large hydrophobic residues in its structure for stability. This paper analyzes the variation of these large hydrophobic residues in different species and its relevance to protein hydration, stability and disease. Protein sequences of 20 different living systems, including human, chimpanzee, dog, cow, mouse, rat, chicken, fruitfly, zebrafish, C.elegan, mosquito, honeybee, beetle, yeast, S. purpuratus, K. lactis, S. pombe and A. thaliana have been analyzed. For comparison the Influenza virus and P. falciparum are studied. The results show that there is reduction of large hydrophobic residues during evolution that causes hydration in proteins. The length of protein sequences increases accordingly. The reduction is high in heterosexual animals than that of plant and fungi. The reduction is observed based on the food habits, sexual behavior and environmental factors of the living system. To conclude many proteins are being hydrated during evolution that cause disease. This is very much in human.
Protein Length, Protein hydration, Protein Evolution, Protein Analysis, disease protein
