Refolding of Cold‐Denatured Barstar Induced by Radio‐Frequency Heating: A New Method to Study Protein Folding by Real‐Time NMR Spectroscopy-Reference-Cited by-同舟云学术

Refolding of Cold‐Denatured Barstar Induced by Radio‐Frequency Heating: A New Method to Study Protein Folding by Real‐Time NMR Spectroscopy

Published:2020-09-25 Issue:49 Volume:59 Page:22086-22091
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Pintér György¹,Schwalbe Harald¹^ORCID

Affiliation:

1. Institute for Organic Chemistry and Chemical Biology Center for Biomolecular Magnetic Resonance (BMRZ) Johann Wolfgang Goethe-Universität Frankfurt Max-von-Laue-Str. 7 60438 Frankfurt Germany

Funder

Deutsche Forschungsgemeinschaft

Horizon 2020 Framework Programme

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.202006945

Reference47 articles.

1. From Levinthal to pathways to funnels

2. NMR spectroscopy brings invisible protein states into focus

3. Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy

4. Following protein folding in real time using NMR spectroscopy

5. Equilibrium and Kinetic Unfolding of GB1: Stabilization of the Native State by Pressure

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