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The unfolding mechanism and the disulfide structures of denatured lysozyme

✍ Scribed by Jui-Yoa Chang; Li Li

Book ID
117103794
Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
206 KB
Volume
511
Category
Article
ISSN
0014-5793

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Comparison between the unfolding rate an
Comparison between the unfolding rate and structural fluctuations in native lysozymeβ€”effects of denaturants, ligand binding, and intrachain cross-linking on hydrogen exchange and unfolding kinetics
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The hydrogen-exchange reactions of peptide NH groups in lysozyme were studied by the change in the intensity of the amide I1 band in the ir spectrum. The slowest exchanging hydrogens, which are involved in intramolecular hydrogen bonding, are further divided into two groups a t lower temperatures; h