A modular approach to map out the conformational landscapes of unbound intrinsically disordered proteins-Reference-Cited by-同舟云学术

A modular approach to map out the conformational landscapes of unbound intrinsically disordered proteins

Published:2022-06-03 Issue:23 Volume:119 Page:
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proc. Natl. Acad. Sci. U.S.A.

Author:

Luong Thinh D. N.¹²,Nagpal Suhani¹³,Sadqi Mourad¹⁴^ORCID,Muñoz Victor¹²³⁴^ORCID

Affiliation:

1. Center for Cellular and Biomolecular Machines, University of California, Merced, CA 95343

2. Chemistry and Biochemistry Graduate Program, University of California, Merced, CA 95343

3. Bioengineering Graduate Program, University of California, Merced, CA 95343

4. Department of Bioengineering, University of California, Merced, CA 95343

Abstract

Significance Intrinsically disordered proteins have the unique ability to morph in response to multiple partners and thereby process sophisticated inputs and outputs. It is, however, a mystery whether their response is passive, that is, entirely determined by the partner, or controlled via an internal, yet unknown, folding mechanism. Here we introduce an approach to examine this key question and demonstrate its potential by dissecting the conformational properties of the partially disordered protein NCBD and obtaining important clues about how it performs its biological function.

Funder

National Science Foundation

W. M. Keck Foundation

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Link

https://pnas.org/doi/pdf/10.1073/pnas.2113572119

Reference62 articles.

1. Principles that Govern the Folding of Protein Chains

2. Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions