Sequence correlations shape protein promiscuity

David B. Lukatsky; Ariel Afek; Eugene I. Shakhnovich

doi:10.1063/1.3624332

Sequence correlations shape protein promiscuity

David B. Lukatsky, Ariel Afek, Eugene I. Shakhnovich

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

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.

Original language	English
Article number	065104
Journal	Journal of Chemical Physics
Volume	135
Issue number	6
DOIs	https://doi.org/10.1063/1.3624332
State	Published - 14 Aug 2011

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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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.",

author = "Lukatsky, {David B.} and Ariel Afek and Shakhnovich, {Eugene I.}",

note = "Funding Information: D.B.L. acknowledges the financial support from the Israel Science Foundation (ISF) Grant 1014/09. A.A. is a recipient of the Lewiner graduate fellowship. ",

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N2 - 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.

AB - 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.

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Sequence correlations shape protein promiscuity

Abstract

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