Issue 14, 1995

Vibrational Raman optical activity of lysozyme: hydrogen–deuterium exchange, unfolding and ligand binding

Abstract

Measurements of the vibrational Raman optical activity (ROA) spectra of hen egg white lysozyme are reported which show that ROA is a useful new probe of protein secondary and tertiary structure and dynamics. ROA spectra can be measured just as easily in D2O as in H2O and a comparison of the two gives information about the relative exchange rates of the amide hydrogens in the peptide backbone for the various types of secondary and tertiary structure in lysozyme. Unfolded lysozyme shows a large conservative ROA couplet in the amide III region which might facilitate the identification of signatures in the ROA spectra of native proteins from irregular structures with the same type of conformational heterogeneity as that of an unfolded protein. The ROA spectrum of lysozyme bound to a saccharide inhibitor shows evidence for an increase in rigid loop content.

Article information

Article type
Paper

J. Chem. Soc., Faraday Trans., 1995,91, 2087-2093

Vibrational Raman optical activity of lysozyme: hydrogen–deuterium exchange, unfolding and ligand binding

S. J. Ford, A. Cooper, L. Hecht, G. Wilson and L. D. Barron, J. Chem. Soc., Faraday Trans., 1995, 91, 2087 DOI: 10.1039/FT9959102087

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements