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

Hunt, N.T. and Kattner, Lisa and Shanks, Richard P. and Wynne, Klaas (2007) The dynamics of water-protein interaction studied by ultrafast optical Kerr-effect spectroscopy. Journal of American Chemical Society, 129 (11). 3168 -3172. ISSN 1520-5126 (http://dx.doi.org/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 -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.

ORCID iDs

Hunt, N.T. ORCID logoORCID: https://orcid.org/0000-0001-7400-5152, Kattner, Lisa, Shanks, Richard P. and Wynne, Klaas ORCID logoORCID: https://orcid.org/0000-0002-5305-5940;
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