The Cold-Unfolded State Is Expanded but Contains Long- and Medium-Range Contacts and Is Poorly Described by Homopolymer Models-Reference-Cited by-同舟云学术

The Cold-Unfolded State Is Expanded but Contains Long- and Medium-Range Contacts and Is Poorly Described by Homopolymer Models

Published:2020-07-31 Issue:36 Volume:59 Page:3290-3299
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Stenzoski Natalie E.¹,Zou Junjie²,Piserchio Andrea³,Ghose Ranajeet³⁴,Holehouse Alex S.⁵⁶^ORCID,Raleigh Daniel P.¹²⁷^ORCID

Affiliation:

1. Graduate Program in Biochemistry & Structural Biology, Stony Brook University, Stony Brook, New York 11794-3400, United States

2. Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, United States

3. Department of Chemistry and Biochemistry, The City College of New York, New York, New York 10031, United States

4. Graduate Programs in Biochemistry, Chemistry and Physics, The Graduate Center of CUNY, New York, New York 10016, United States

5. Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States

6. Center for Science and Engineering of Living Systems, Department of Biomedical Engineering, Washington University in St. Louis, St. Louis, Missouri 63130, United States

7. Institute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, United Kingdom

Funder

Division of Molecular and Cellular Biosciences

Wellcome Trust

Division of Physics

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00469

Reference81 articles.

1. Theory for the folding and stability of globular proteins

2. Polymer principles and protein folding

3. Relating sequence encoded information to form and function of intrinsically disordered proteins

4. Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions

5. Classification of Intrinsically Disordered Regions and Proteins

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