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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.||
Qin, Sanbo, author
Zhou, Huan-Xiang, author
|Type of Resource:||text|
|Extent:||1 online resource|
|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.|
|Persistent Link to This Record:||http://purl.flvc.org/fsu/fd/FSU_pmch_27771543|
|Is Part Of:||
Current opinion in structural biology.
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