%0 Journal Article
%T COMPARATIVE ANALYSIS ON LARGE HYDROPHOBIC RESIDUES AND SMALL HYDROPHOBIC RESIDUES IN DIFFERENT ORGANISMS
%A VINOBHA CS
%A VINOBHA CS
%J International Journal of Bioinformatics Research
%D 2011
%I Bioinfo Publications
%X One of the major tasks carried by biologist today is to understand the nature of proteins. How this largeprotein molecule folds themselves into some form and carryout the prescribed biochemical reactions.Hydrophobic interaction is the dominant force towards this task. To understand this interaction, a simple statisticalanalysis on the contribution of hydrophobic residues was carried out. Large Hydrophobic Residues (LHR) such asPhenylalanine (F), Isoleucine (I), Leucine (L), Methionine (M) and Valine (V) ¨C (FILMV) as well as smallhydrophobic residues (SHR) Glycine (G), Alanine (A), Proline (P), Cysteine (C) and Tryptophan (W) - (GAPCW)were studied in all proteins of given organisms. The organisms include Homo sapiens, Macaca Mullatta, Pantroglodytes, Canis familiaris, Gallus gallus, Mus musculus, Rattus norvegicus, Bos taurus, Drosophilamelonogaster, Monodelphis domestica, Danio rerio, Stronglycentrolus purpuratus, Anopheles gambiae, Apismellifera, Arabidopsis thaliana, Tribolium castaneum, Saccharomyces cerevisae, Schizosaccharomyces pombeand Caenorhabditis elegans. It is observed that the protein prefers to have 27% large hydrophobic residues tomaintain the required hydrophobicity. In animal, particularly in human, it is observed less. It is interesting to notethat small hydrophobic residues balance this lack in number by a factor of 1:3. So is the reason why the length ofthe animal proteins increases. This new finding on the contribution of hydrophobic residues in protein stability willbe discussed in detail
%K proteomics
%K hydrophobicity analysis
%K large hydrophobic residues
%K small hydrophobic residues
%K sequence analysis
%K bioinformatics
%U http://www.bioinfo.in/uploadfiles/12938085363_1_2_IJBR.pdf