title: Sequence correlations shape protein promiscuity.
abstract: We predict analytically that diagonal correlations of amino acid positions within protein sequences statistically enhance protein propensity for nonspecific binding. We use the term "promiscuity" to describe such nonspecific binding. Diagonal correlations represent statistically significant repeats of sequence patterns where amino acids of the same type are clustered together. The predicted effect is qualitatively robust with respect to the form of the microscopic interaction potentials and the average amino acid composition. Our analytical results provide an explanation for the enhanced diagonal correlations observed in hubs of eukaryotic organismal proteomes [J. Mol. Biol. 409, 439 (2011)]. We suggest experiments that will allow direct testing of the predicted effect.
authors.affiliation: Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel. lukatsky@bgu.ac.il
authors.forename: David B
authors.initials: DB
authors.lastname: Lukatsky
authors.forename: Ariel
authors.initials: A
authors.lastname: Afek
authors.forename: Eugene I
authors.initials: EI
authors.lastname: Shakhnovich
mesh_terms: D000595:Amino Acid Sequence; D056890:Eukaryota; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D020543:Proteome
chemical_list: D011506:Proteins; D020543:Proteome