Role of large hydrophobic residues in proteins

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.

MAGNITUDE OF THYMINE IN DIFFERENT FRAMES OF MESSENGER RNAs

“…The earlier works on thymine distribution conclude that frame 1 should have definite amount thymine for translating mRNA into proteins with adequate large hydrophobic residues for defined carbon content [1,4]. It is confirmed the same in different species studied here.…”

Critical Roles of Two Hydrophobic Residues within Human Glucose Transporter 9 (hSLC2A9) in Substrate Selectivity and Urate Transport

“…Residues such as isoleucine, valine, leucine, and phenylalanine are often clustered within active sites (29). For example, SLC2A1 has a leucine (Leu-279) within the most conserved motif QLS in GLUTs adjacent to the postulated "bottle-neck" region of the substrate transport pathway (30), and valine 165 is also predicted to be located near the exofacial surface of the substrate binding site (31).…”

Molecular conformation of linear alkane molecules: From gas phase to bulk water through the interface

“…This is due to the large number of studied systems , which are of interest for technology, as well as those related to biomatter processes, where it is frequent to encounter many hydrophobic molecules which are in contact with water, or in general with aqueous systems. Also the importance of hydrophobic moieties for stabilizing protein structures and their structurally stable conformation, thus permitting enzymatic processes to occur, is accepted; this is especially valid for membrane proteins 1 . Hydrophobic molecules penetrating through the waterhydrophobic interface is an important process to stabilize the protein conformation 2 ; hence the protein's stable structure results from hydrophobic interactions 3 .…”