Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00567a027
Reference35 articles.
1. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
2. Role of proline isomerization in folding of ribonuclease A at low temperatures
3. Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor
4. MEASUREMENT OF STRUCTURAL AND FREE ENERGY CHANGES IN HEMOGLOBIN BY HYDROGEN EXCHANGE METHODS
5. Hydrogen-tritium exchange of the random chain polypeptide
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