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Title
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Role of large hydrophobic residues in proteins
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Authors
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Veerasamy Jayaraj, Ramamoorthi Suhanya, Marimuthu Vijayasarathy, Perumal Anandagopu and Ekambaram Rajasekaran*
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Affiliation |
Department of Biotechnology and Computer Application, Periyar Maniammai University, Thanjavur - 613403, Tamil Nadu, India
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Article Type |
Hypothesis
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Date
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received January 05, 2009; revised March 07, 2009; accepted April 16, 2009; published June 13, 2009
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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.
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Keywords
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LHR; Large Hydrophobic Residues; Protein Analysis; Sequence Analysis
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Citation |
Jayaraj et al, Bioinformation 3(9): 409-412 (2009)
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Edited by |
P. Kangueane
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ISSN |
0973-2063
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Publisher |
Biomedical Informatics
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License
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This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
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