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

N.T. Hunt, Lisa Kattner, Richard P. Shanks, Klaas Wynne

Research output: Contribution to journalArticle

68 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)3168 -3172
JournalJournal of American Chemical Society
Volume129
Issue number11
DOIs
Publication statusPublished - 2007

Keywords

  • nanoscience
  • applied physics
  • spectroscopy
  • raman spectrum
  • proteins

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