Protein folding kinetics from magnetization transfer nuclear magnetic resonance-Reference-Cited by-同舟云学术

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Protein folding kinetics from magnetization transfer nuclear magnetic resonance

Published:1984-09-11 Issue:19 Volume:23 Page:4267-4270
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dobson Christopher M.,Evans Philip A.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00314a001

Reference30 articles.

1. Nuclear magnetic resonance studies of the unfolding of pancreatic ribonuclease

2. Crystallographic studies of the activity of hen egg-white lysozyme

3. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

4. Nuclear magnetic resonance studies on the structure of lysozyme in solution

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1. On the potential of Fourier-encoded saturation transfers for sensitizing solid-state magic-angle spinning NMR experiments;The Journal of Chemical Physics;2022-02-07

2. Monitoring protein unfolding transitions by NMR-spectroscopy;Journal of Biomolecular NMR;2022-01-04

3. NMR Spectroscopy and Protein Folding: Studies of Lysozyme and α-Lactalbumin;Ciba Foundation Symposium 161 - Protein Conformation;2007-09-28

4. Proteins and Protein Fragments: Folding;Encyclopedia of Magnetic Resonance;2007-03-15

5. Millisecond Protein Folding Studied by NMR Spectroscopy;Protein & Peptide Letters;2005-02-01

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