Role of large hydrophobic residues in proteins

Veerasamy Jayaraj,Perumal Anandagopu,Ekambaram Rajasekaran,Marimuthu Vijayasarathy,Ramamoorthi Suhanya

doi:10.6026/97320630003409

Abstract

Large Hydrophobic Residues (LHR) such as phenylalanine, isoleucine, leucine, methionine and valine play an important role in protein structure and activity. We describe the role of LHR in complete set of protein sequences in 15 different species. That is the distribution of LHR in different proteins of different species is reported. It is observed that the proteins prefer to have 27% of large hydrophobic residues in total and all along the sequence. It is also observed that proteins accumulate more LHR in its active sites. A window analysis on these protein sequences shows that the 27% of LHR is more frequent at window length of 45 amino acids. The influenza virus and P. falciparum show a random distribution of LHR in its proteins compared to other model organisms.

Highlights

Proteins are the working force in all living systems
The shortage of Large Hydrophobic Residues (LHR) in animals is balanced by adding more number of small hydrophobic residues such as Brooks et al [7] reported the evolution of amino acid Glycine, Alanine, Proline and Cysteine
The (X= A, T, G or C) [8] that code for only Large probable amounts of LHR for different window lengths in Hydrophobic Residues (LHR) such as phenylalanine, all 15 species are plotted in figure 2

Summary

Introduction

Proteins are the working force in all living systems. These Methodology: proteins that are translated from mRNA are evolved to Dataset have a defined structure and specified function. White and Jacobs [6] reported the statistical distribution the number of LHR residues in a defined window length of hydrophobic residues along the protein chains and its (number of amino acids between 10 and 100) counted and implications to protein folding and evolution. The amount of LHR at tested for randomness of hydrophobic residues in the which there is a maximum number of windows is taken as proteins with limited sequences.

Results

Conclusion