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Biophysical Journal 85:1903-1913 (2003)
© 2003 The Biophysical Society

Low-Frequency Modes of Peptides and Globular Proteins in Solution Observed by Ultrafast OHD-RIKES Spectroscopy

Gerard Giraud, Jan Karolin and Klaas Wynne

Department of Physics, University of Strathclyde, Glasgow G4 0NG, Scotland, United Kingdom

Correspondence: Address reprint requests to Klaas Wynne, 107 Rottenrow, Glasgow G4 0NG, Scotland, UK. Tel.: 44-141-548-3381; E-mail: klaas.wynne{at}phys.strath.ac.uk.

The low-frequency (1–200 cm-1) 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 {alpha}-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, {alpha}-lactalbumin, pepsin, and ß-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.




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