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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 Hore
Photo-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.

History

Publication status

  • Published

Journal

Journal of Biomolecular NMR

ISSN

1573-5001

Publisher

Springer Verlag

Issue

2

Volume

44

Page range

77-86

Department affiliated with

  • Chemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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