Sequence correlations shape protein promiscuity

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

Research output: Contribution to journalArticlepeer-review

8 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 languageEnglish
Article number065104
JournalJournal of Chemical Physics
Volume135
Issue number6
DOIs
StatePublished - 14 Aug 2011

ASJC Scopus subject areas

  • Physics and Astronomy (all)
  • Physical and Theoretical Chemistry

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