Line Shape Analysis of <sup>19</sup>F NMR-Monitored Chemical Denaturation of a Fold-Switching Protein RfaH Reveals Its Slow Folding Dynamics-Reference-Cited by-同舟云学术

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Line Shape Analysis of ¹⁹F NMR-Monitored Chemical Denaturation of a Fold-Switching Protein RfaH Reveals Its Slow Folding Dynamics

Published:2023-11-22 Issue:2 Volume:128 Page:465-471
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Bhuvaneshwari R. Aishwarya¹,Shivamani Anish¹,Sengupta Ishita¹^ORCID

Affiliation:

1. Department of Chemistry, IIT Bombay, Powai, Mumbai 400076, India

Funder

Council of Scientific and Industrial Research, India

Science and Engineering Research Board

Industrial Research and Consultancy Centre

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.3c06550

Reference39 articles.

1. Dissecting the Dynamic Conformations of the Metamorphic Protein Lymphotactin

2. Structural Basis for Converting a General Transcription Factor into an Operon-Specific Virulence Regulator

3. An α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation Factor

4. Structural Basis for Transcript Elongation Control by NusG Family Universal Regulators

5. Energy Landscape for Fold-Switching in Regulatory Protein RfaH

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1. Metamorphic proteins and how to find them;Current Opinion in Structural Biology;2024-06

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