Atomistic Modeling of Intrinsically Disordered Proteins Under Polyethylene Glycol Crowding: Quantitative Comparison with Experimental Data and Implication of Protein–Crowder Attraction-Reference-Cited by-同舟云学术

Atomistic Modeling of Intrinsically Disordered Proteins Under Polyethylene Glycol Crowding: Quantitative Comparison with Experimental Data and Implication of Protein–Crowder Attraction

Published:2018-09-19 Issue:49 Volume:122 Page:11262-11270
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Nguemaha Valery¹,Qin Sanbo¹,Zhou Huan-Xiang¹²^ORCID

Affiliation:

1. Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, United States

2. Department of Chemistry and Department of Physics, University of Illinois at Chicago, Chicago, Illinois 60607, United States

Funder

National Institute of General Medical Sciences

US-Israel Binational Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.8b07066

Reference50 articles.

1. Flexible nets. The roles of intrinsic disorder in protein interaction networks

2. Intrinsic disorder: signaling via highly specific but short-lived association

3. Intrinsic disorder in cell signaling and gene transcription

4. Intrinsically disordered proteins in cellular signalling and regulation

5. Structure of Cdc42 in complex with the GTPase-binding domain of the ‘Wiskott–Aldrich syndrome’ protein

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