Evidence for a new cooperative transition in native lysozyme from temperature-dependent Raman optical activity

Wilson, G., Hecht, L. and Barron, L. D. (1997) Evidence for a new cooperative transition in native lysozyme from temperature-dependent Raman optical activity. Journal of Physical Chemistry B, 101(4), pp. 694-698. (doi: 10.1021/jp962480f)

Full text not currently available from Enlighten.

Abstract

On account of its special sensitivity to conformational mobility in chiral molecular structure, vibrational Raman optical activity has revealed what appears to be a new type of sharp cooperative transition in a native protein, possibly related to its function, from measurements on hen egg white lysozyme in the temperature range 2−50 °C. It occurs at ∼12 °C and involves the loss of residual mobility in tertiary loop and secondary structure and, in tryptophan side groups, in both domains of the protein including the active site region. No significant conformational change appears to be involved. Since differential scanning calorimetry failed to reveal any latent heat, it does not appear to be a simple first-order phase transition.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Hecht, Dr Lutz and Barron, Professor Laurence
Authors: Wilson, G., Hecht, L., and Barron, L. D.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Journal of Physical Chemistry B
Publisher:American Chemical Society
ISSN:1520-6106
ISSN (Online):1520-5207

University Staff: Request a correction | Enlighten Editors: Update this record