Biography
Biography: Perumal Ananda Gopu
Abstract
In the present study, the protein sequences have been preconceived in series of atoms instead of amino acids (AA). Specifically, the stretches of protein sequences have been considered preferably in terms of carbon atoms instead of using an AA-based pattern. Accordingly, we have observed that patterns consisting of the same number of carbons can result in different AA lengths with different numbers of total atoms. The variation of these patterns is characterized by a change in the distribution of large hydrophobic residues (LHRs) (such as phenylalanine, isoleucine, leucine, methionine and valine) with the introduction of higher numbers of small hydrophobic residues (SHRs), such as glycine, alanine, proline and cysteine. Consequently, proteins that have the same number of carbons can have different numbers of AA within their various patterns and thus an increase in their peptide length. Hence, proteins of the same carbon contents may show different patterns with different peptide lengths that may reflect their specific biological functions. Concluding, an atomic level comparison of protein sequences can provide better results than a similar comparison at the residues level which may have potential implications for the prediction of misfolded proteins.