Weak Chemical Interactions That Drive Protein Evolution: Crowding, Sticking, and Quinary Structure in Folding and Function-Reference-Cited by-同舟云学术

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Weak Chemical Interactions That Drive Protein Evolution: Crowding, Sticking, and Quinary Structure in Folding and Function

Published:2019-07-29 Issue:18 Volume:119 Page:10691-10717
ISSN:0009-2665
Container-title:Chemical Reviews
language:en
Short-container-title:Chem. Rev.

Author:

Guin Drishti¹,Gruebele Martin¹²³^ORCID

Affiliation:

1. Department of Chemistry, University of Illinois, Urbana, Illinois 61801, United States

2. Department of Physics, University of Illinois, Urbana, Illinois 61801, United States

3. Center for Biophysics and Quantitative Biology, University of Illinois, Urbana, Illinois 61801, United States

Funder

Division of Molecular and Cellular Biosciences

Publisher

American Chemical Society (ACS)

Subject

General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.chemrev.8b00753

Reference284 articles.

1. Dissociation of the Tubulin Dimer Is Extremely Slow, Thermodynamically Very Unfavorable, and Reversible in the Absence of an Energy Source

2. Evolutionary meandering of intermolecular interactions along the drift barrier

3. Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences

4. Is the depletion force entropic? Molecular crowding beyond steric interactions

5. A cell is more than the sum of its (dilute) parts: A brief history of quinary structure

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