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 0006-3495Full text not available in this repository. (Request a copy from the Strathclyde author)
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.
|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:||29 Apr 2016 07:35|