Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditions in vitro and in cells-Reference-Cited by-同舟云学术

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Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditions in vitro and in cells

Published:2023-11 Issue:4 Volume:3 Page:319-326
ISSN:2772-5162
Container-title:Magnetic Resonance Letters
language:en
Short-container-title:Magnetic Resonance Letters

Author:

Chu I-Te,Pielak Gary J.^ORCID

Funder

National Science Foundation

Publisher

Elsevier BV

Subject

General Medicine

Reference107 articles.

1. Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs);Theillet;Chem. Rev.,2014

2. Protein stability and weak intracellular interactions;Guseman,2020

3. Excluded volume as a determinant of macromolecular structure and reactivity;Minton;Biopolymers,1981

4. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli;Zimmerman;J. Mol. Biol.,1991

5. Protein-binding dynamics imaged in a living cell;Phillip;Proc. Natl. Acad. Sci. U.S.A.,2012

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