Native state volume fluctuations in proteins as a mechanism for dynamic allostery

Law, Anthony B.; Sapienza, Paul J.; Zhang, Jun; Zuo, Xiaobing; Petit, Chad M.

doi:10.1021/jacs.6b12058

Title: Native state volume fluctuations in proteins as a mechanism for dynamic allostery

Journal Article · Tue Jan 17 00:00:00 EST 2017 · Journal of the American Chemical Society

DOI:https://doi.org/10.1021/jacs.6b12058· OSTI ID:1373407

Law, Anthony B. ^[1]; Sapienza, Paul J. ^[2]; Zhang, Jun ^[3]; Zuo, Xiaobing ^[4];

^[3]

Univ. of Washington, Seattle, WA (United States)
Univ. of North Carolina, Chapel Hill, NC (United States)
Univ. of Alabama, Birmingham, AL (United States)
Argonne National Lab. (ANL), Argonne, IL (United States)

Allostery enables tight regulation of protein function in the cellular environment. While existing models of allostery are firmly rooted in the current structure-function paradigm, the mechanistic basis for allostery in the absence of structural change remains unclear. In this study, we show that a typical globular protein is able to undergo significant changes in volume under native conditions while exhibiting no additional changes in protein structure. These native state volume fluctuations were found to correlate with changes in internal motions that were previously recognized as a source of allosteric entropy. This finding offers a novel mechanistic basis for allostery in the absence of canonical structural change. As a result, the unexpected observation that function can be derived from expanded, low density protein states has broad implications for our understanding of allostery and suggests that the general concept of the native state be expanded to allow for more variable physical dimensions with looser packing.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1373407

Journal Information:: Journal of the American Chemical Society, Vol. 139, Issue 10; ISSN 0002-7863

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 29 works

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