Year: 2011
Type: article
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.
Source: The Journal of Chemical Physics
DOI: 10.1063/1.3624332
Institutions: Ben-Gurion University of the Negev, Harvard University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Funder: Israel Science Foundation
Award: G2301598311
OpenAlex ID: W1997279188