000114838 001__ 114838
000114838 005__ 20181203021031.0
000114838 0247_ $$2doi$$a10.1093/protein/5.8.729
000114838 037__ $$aARTICLE
000114838 245__ $$aQuantile distributions of amino acid usage in protein classes
000114838 269__ $$a1992
000114838 260__ $$c1992
000114838 336__ $$aJournal Articles
000114838 500__ $$aDepartment of Mathematics, Stanford University, CA 94305.
000114838 520__ $$aA comparative study of the compositional properties of various protein sets from both cellular and viral organisms is presented. Invariants and contrasts of amino acid usages have been discerned for different protein function classes and for different species using robust statistical methods based on quantile distributions and stochastic ordering relationships. In addition, a quantitative criterion to assess amino acid compositional extremes relative to a reference protein set is proposed and applied. Invariants of amino acid usage relate mainly to the central range of quantile distributions, whereas contrasts occur mainly in the tails of the distributions, especially contrasts between eukaryote and prokaryote species. Influences from genomic constraint are evident, for example, in the arginine:lysine ratios and the usage frequencies of residues encoded by G + C-rich versus A + T-rich codon types. The structurally similar amino acids, glutamate versus aspartate and phenylalanine versus tyrosine, show stochastic dominance relationships for most species protein sets favoring glutamate and phenylalanine respectively. The quantile distribution of hydrophobic amino acid usages in prokaryote data dominates the corresponding quantile distribution in human data. In contrast, glutamate, cysteine, proline and serine usages in human proteins dominate the corresponding quantile distributions in Escherichia coli. E. coli dominates human in the use of basic residues, but no dominance ordering applies to acidic residues. The discussion centers on commonalities and anomalies of the amino acid compositional spectrum in relation to species, function, cellular localization, biochemical and steric attributes, complexity of the amino acid biosynthetic pathway, amino acid relative abundances and founder effects.
000114838 700__ $$aKarlin, S.
000114838 700__ $$aBlaisdell, B. E.
000114838 700__ $$0244404$$aBucher, P.$$g113607
000114838 773__ $$j5$$k8$$q729-38$$tProtein Eng
000114838 909C0 $$0252244$$pGR-BUCHER$$xU11780
000114838 909CO $$ooai:infoscience.tind.io:114838$$pSV$$particle
000114838 937__ $$aGR-BUCHER-ARTICLE-1992-002
000114838 973__ $$aOTHER$$rREVIEWED$$sPUBLISHED
000114838 980__ $$aARTICLE