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Nmr studies on the induced denaturation of lysozyme by guanidine hydrochloride in the presence of the inhibitor (NAG)3

โœ Scribed by M. Sheinblatt

Publisher
Wiley (John Wiley & Sons)
Year
1989
Tongue
English
Weight
560 KB
Volume
28
Category
Article
ISSN
0006-3525

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โœฆ Synopsis

The stabilization of the folded conformation of lysozyme, arising from the binding of the inhibitor (NAG) against induced denaturation, is demonstrated from the 'H-nmr spectra of the enzyme. The nmr spectra reveal that the binding of the denaturant (GuHC1) to the enzyme is associbted with changes in the conformation of the enzyme. The binding site of the inhibitor site C also,serves as one of the binding sites of GuHCl. The observation that higher denaturant concentrations are required in the unfolding of Lys-(NAG),, as compared t o free Lys can be explained partly in terms of the existence of a competitive binding to the enzyme involving the (NAG) and GuHCI molecules.

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