The dynamics of water-protein interaction studied by ultrafast optical kerr-effect spectroscopy

Hunt, N. T., Kattner, L., Shanks, R. P. and Wynne, K. (2007) The dynamics of water-protein interaction studied by ultrafast optical kerr-effect spectroscopy. Journal of the American Chemical Society, 129(11), pp. 3168-3172. (doi:10.1021/ja066289n)

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Abstract

Changes in the ultrafast dynamics and terahertz Raman spectrum accompanying a helix-to-coil transition of a homo-polypeptide have been observed for the first time. Formation of the α-helix is associated with a shift to lower frequency of a broad Raman band attributable to solvent-peptide intermolecular hydrogen bonding. This band facilitates direct spectroscopic observation of so-called hydration water near a peptide and yields the first quantitative estimate of the time scale of the ultrafast dynamics in the solvation shell, which range from 0.18 to 0.33 ps (185−100 cm-1) depending on the secondary structure of the peptide. Such fast motions of solvent molecules have been referred to as the “lubricant of life” and are thought to play key roles in determining structure and activity of proteins.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Shanks, Dr Richard and Wynne, Professor Klaas
Authors: Hunt, N. T., Kattner, L., Shanks, R. P., and Wynne, K.
Subjects:Q Science > QD Chemistry
College/School:College of Science and Engineering > School of Chemistry
College of Science and Engineering > Scottish Universities Environmental Research Centre
Journal Name:Journal of the American Chemical Society
Publisher:American Chemical Society
ISSN:0002-7863
ISSN (Online):1520-5126
Published Online:23 February 2007

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