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Role of large hydrophobic residues in proteins

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...

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Autores principales: Jayaraj, Veerasamy, Suhanya, Ramamoorthi, Vijayasarathy, Marimuthu, Anandagopu, Perumal, Rajasekaran, Ekambaram
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics Publishing Group 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2732037/
https://www.ncbi.nlm.nih.gov/pubmed/19759817
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author Jayaraj, Veerasamy
Suhanya, Ramamoorthi
Vijayasarathy, Marimuthu
Anandagopu, Perumal
Rajasekaran, Ekambaram
author_facet Jayaraj, Veerasamy
Suhanya, Ramamoorthi
Vijayasarathy, Marimuthu
Anandagopu, Perumal
Rajasekaran, Ekambaram
author_sort Jayaraj, Veerasamy
collection PubMed
description 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.
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spelling pubmed-27320372009-09-16 Role of large hydrophobic residues in proteins Jayaraj, Veerasamy Suhanya, Ramamoorthi Vijayasarathy, Marimuthu Anandagopu, Perumal Rajasekaran, Ekambaram Bioinformation Hypothesis 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. Biomedical Informatics Publishing Group 2009-06-13 /pmc/articles/PMC2732037/ /pubmed/19759817 Text en © 2009 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Jayaraj, Veerasamy
Suhanya, Ramamoorthi
Vijayasarathy, Marimuthu
Anandagopu, Perumal
Rajasekaran, Ekambaram
Role of large hydrophobic residues in proteins
title Role of large hydrophobic residues in proteins
title_full Role of large hydrophobic residues in proteins
title_fullStr Role of large hydrophobic residues in proteins
title_full_unstemmed Role of large hydrophobic residues in proteins
title_short Role of large hydrophobic residues in proteins
title_sort role of large hydrophobic residues in proteins
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2732037/
https://www.ncbi.nlm.nih.gov/pubmed/19759817
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