Publication:

Sequence correlations shape protein promiscuity

Thumbnail Image

Open/View Files

106683 1004.5048.pdf (2.18 MB)

Date

2011

Authors

Published Version

10.1063/1.3624332

Journal Title

Journal ISSN

Volume Title

Publisher

AIP Publishing
The Harvard community has made this article openly available. Please share how this access benefits you.

Research Projects

Organizational Units

Journal Issue

Citation

Lukatsky, David B., Ariel Afek, and Eugene I. Shakhnovich. 2011. “Sequence Correlations Shape Protein Promiscuity.” The Journal of Chemical Physics135 (6): 065104. https://doi.org/10.1063/1.3624332.

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.

Description

Other Available Sources

Research Data

Keywords

Terms of Use

This article is made available under the terms and conditions applicable to Open Access Policy Articles (OAP), as set forth at Terms of Service

URI

http://nrs.harvard.edu/urn-3:HUL.InstRepos:41534238

Collections

FAS Scholarly Articles

Endorsement

Review

Supplemented By

Related Stories