000114840 001__ 114840
000114840 005__ 20190527151552.0
000114840 0247_ $$2doi$$a10.1073/pnas.89.24.12165
000114840 037__ $$aARTICLE
000114840 245__ $$aCorrelation analysis of amino acid usage in protein classes
000114840 269__ $$a1992
000114840 260__ $$c1992
000114840 336__ $$aJournal Articles
000114840 500__ $$aDepartment of Mathematics, Stanford University, CA 94305.
000114840 520__ $$aWe present a comparative study of residue usage correlations of various organism protein sets of diverse phylogenetic species and of open reading frames of several large human viral genomes. Our correlation analysis reveals three major tendencies: (i) charge compensation reflected by the high correlation of basic with acidic residues; (ii) the positive correlations of functionally and structurally similar amino acids including many pairs of hydrophobic amino acids, all pairs of aromatic amino acids, the anionic pair (glutamate and aspartate), but not the cationic pair (lysine and arginine), moderately the hydroxyl pair (serine and threonine), the small amino acids (glycine and alanine), and many (but not all) of those having high values in the Dayhoff substitutability matrix (characteristics such as amino acid polarity or codon usage agreement, except for the wobble position, do not necessarily imply significant positive correlations); (iii) a widespread negative correlation of the aggregate strong codon group amino acids (Ala, Gly, Pro) versus the weak codon group amino acids (Lys, Ile, Tyr, Asn, Phe). Discussion and speculations relate amino acid usage correlations to protein function/structure, cellular localization, proximity in amino acid biosynthetic pathways, amino acid relative abundances, tRNA and aminoacyl synthetase availabilities, and evolutionary processes.
000114840 700__ $$aKarlin, S.
000114840 700__ $$g113607$$aBucher, P.$$0244404
000114840 773__ $$j89$$tProceedings Of The National Academy Of Sciences Of The United States Of America$$k24$$q12165-9
000114840 909C0 $$xU11780$$0252244$$pGR-BUCHER
000114840 909CO $$pSV$$particle$$ooai:infoscience.tind.io:114840
000114840 937__ $$aGR-BUCHER-ARTICLE-1992-004
000114840 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000114840 980__ $$aARTICLE