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Refolding of Ribonuclease A monitored by real-time photo-CIDNP NMR spectroscopy
journal contribution
posted on 2023-06-08, 00:04 authored by Iain Day, Kiminori Maeda, Howard J Paisley, K Hun Mok, P J HorePhoto-CIDNP NMR spectroscopy is a powerful method for investigating the solvent accessibility of histi- dine, tyrosine and tryptophan residues in a protein. When coupled to real-time NMR, this technique allows changes in the environments of these residues to be used as a probe of protein folding. In this paper we describe experiments performed to monitor the refolding of ribonuclease A fol- lowing dilution from a high concentration of chemical denaturant. These experiments provide a good example of the utility of this technique which provides information that is difficult to obtain by other biophysical methods. Real- time photo-CIDNP measurements yield residue-specific kinetic data pertaining to the folding reaction, interpreted in terms of current knowledge of the folding of bovine pancreatic ribonuclease A.
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Publication status
- Published
Journal
Journal of Biomolecular NMRISSN
1573-5001Publisher
Springer VerlagExternal DOI
Issue
2Volume
44Page range
77-86Department affiliated with
- Chemistry Publications
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- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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