Refolding of ribonuclease A monitored by real-time photo-CIDNP NMR spectroscopy |
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| Authors: | Iain J Day Kiminori Maeda Howard J Paisley K Hun Mok P J Hore |
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| Institution: | (1) Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK;(2) Present address: Department of Chemistry and Biochemistry, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9QJ, UK;(3) Present address: Trinity College, School of Biochemistry and Immunology, University of Dublin, Dublin 2, Ireland |
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| Abstract: | Photo-CIDNP NMR spectroscopy is a powerful method for investigating the solvent accessibility of histidine, 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 following 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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| Keywords: | Photo-CIDNP Real-time NMR Protein folding Ribonuclease A |
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