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Protein folding, binding, and droplet formation in cell-like conditions.

Title: Protein folding, binding, and droplet formation in cell-like conditions.
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Name(s): Qin, Sanbo, author
Zhou, Huan-Xiang, author
Type of Resource: text
Genre: Journal Article
Text
Date Issued: 2017-04-01
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: The many bystander macromolecules in the crowded cellular environments present both steric repulsion and weak attraction to proteins undergoing folding or binding and hence impact the thermodynamic and kinetic properties of these processes. The weak but nonrandom binding with bystander macromolecules may facilitate subcellular localization and biological function. Weak binding also leads to the emergence of a protein-rich droplet phase, which has been implicated in regulating a variety of cellular functions. All these important problems can now be addressed by realistic modeling of intermolecular interactions. Configurational sampling of concentrated protein solutions is an ongoing challenge.
Identifier: FSU_pmch_27771543 (IID), 10.1016/j.sbi.2016.10.006 (DOI), PMC5397379 (PMCID), 27771543 (RID), 27771543 (EID), S0959-440X(16)30169-5 (PII)
Grant Number: R01 GM088187, R35 GM118091
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5397379.
Subject(s): Cells/metabolism
Protein Binding
Protein Folding
Proteins/chemistry
Proteins/metabolism
Substrate Specificity
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_pmch_27771543
Owner Institution: FSU
Is Part Of: Current opinion in structural biology.
1879-033X
Issue: vol. 43

Choose the citation style.
Qin, S., & Zhou, H. -X. (2017). Protein folding, binding, and droplet formation in cell-like conditions. Current Opinion In Structural Biology. Retrieved from http://purl.flvc.org/fsu/fd/FSU_pmch_27771543