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research article

Correlation analysis of amino acid usage in protein classes

Karlin, S.
•
Bucher, P.  
1992
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS)

We present a comparative study of residue usage correlations of various organism protein sets of diverse phylogenetic species and of open reading frames of several large human viral genomes. Our correlation analysis reveals three major tendencies: (i) charge compensation reflected by the high correlation of basic with acidic residues; (ii) the positive correlations of functionally and structurally similar amino acids including many pairs of hydrophobic amino acids, all pairs of aromatic amino acids, the anionic pair (glutamate and aspartate), but not the cationic pair (lysine and arginine), moderately the hydroxyl pair (serine and threonine), the small amino acids (glycine and alanine), and many (but not all) of those having high values in the Dayhoff substitutability matrix (characteristics such as amino acid polarity or codon usage agreement, except for the wobble position, do not necessarily imply significant positive correlations); (iii) a widespread negative correlation of the aggregate strong codon group amino acids (Ala, Gly, Pro) versus the weak codon group amino acids (Lys, Ile, Tyr, Asn, Phe). Discussion and speculations relate amino acid usage correlations to protein function/structure, cellular localization, proximity in amino acid biosynthetic pathways, amino acid relative abundances, tRNA and aminoacyl synthetase availabilities, and evolutionary processes.

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Type
research article
DOI
10.1073/pnas.89.24.12165
Author(s)
Karlin, S.
Bucher, P.  
Date Issued

1992

Publisher

National Academy of Sciences

Published in
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS)
Volume

89

Issue

24

Start page

12165

End page

9

Note

Department of Mathematics, Stanford University, CA 94305.

Editorial or Peer reviewed

REVIEWED

Written at

OTHER

EPFL units
GR-BUCHER  
Available on Infoscience
December 17, 2007
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/15657
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