Low-frequency modes of peptides and globular proteins in solution observed by ultrafast OHD-RIKES Spectroscopy

Giraud, Gerard and Karolin, Jan and Wynne, Klaas (2003) Low-frequency modes of peptides and globular proteins in solution observed by ultrafast OHD-RIKES Spectroscopy. Biophysical Journal, 85 (3). pp. 1903-1913. ISSN 0006-3495 (http://www.biophysj.org/cgi/reprint/85/3/1903)

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Abstract

The low-frequency (1-200 cm1) vibrational spectra of peptides and proteins in solution have been investigated with ultrafast optical heterodyne-detected Raman-induced Kerr-effect spectroscopy (OHD-RIKES). Spectra have been obtained for di-L-alanine (ALA(2)) and the a-helical peptide poly-L-alanine (PLA) in dichloroacetic acid solution. The poly-L-alanine spectrum shows extra amplitude compared to the di-L-alanine spectrum, which can be explained by the secondary structure of the former. The globular proteins lysozyme, a-lactalbumin, pepsin, and b-lactoglobulin in aqueous solution have been studied to determine the possible influence of secondary or tertiary structure on the low-frequency spectra. The spectra of the globular proteins have been analyzed in terms of three nondiffusive Brownian oscillators. The lowest frequency oscillator corresponds to the so-called Boson peak observed in inelastic neutron scattering (INS). The remaining two oscillators are not observed in inelastic neutron scattering, do therefore not involve significant motion of hydrogen atoms, and may be associated with delocalized backbone torsions.

ORCID iDs

Giraud, Gerard, Karolin, Jan and Wynne, Klaas ORCID logoORCID: https://orcid.org/0000-0002-5305-5940;
  • Item type:Article
    ID code:3098
    Dates:
    Date
    Event
    September 2003
    Published
    Keywords:peptides, globular proteins, ultrafast OHD-RIKES, spectroscopy, nanoscience, Solid state physics. Nanoscience, Biophysics
    Subjects:Science > Physics > Solid state physics. Nanoscience
    Department:Faculty of Science > Physics
    Depositing user: Strathprints Administrator
    Date deposited:02 Apr 2007
    Last modified:19 May 2023 01:01
    URI:https://strathprints.strath.ac.uk/id/eprint/3098
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