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

Gerard Giraud, Jan Karolin, Klaas Wynne

Research output: Contribution to journalArticle

107 Citations (Scopus)

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.
LanguageEnglish
Pages1903-1913
Number of pages10
JournalBiophysical Journal
Volume85
Issue number3
Publication statusPublished - Sep 2003

Fingerprint

Spectrum Analysis
Neutrons
Alanine
Peptides
Dichloroacetic Acid
Lactalbumin
Lactoglobulins
Proteins
Pepsin A
Muramidase
Hydrogen
polyalanine
peptide L

Keywords

  • peptides
  • globular proteins
  • ultrafast OHD-RIKES
  • spectroscopy
  • nanoscience

Cite this

Giraud, Gerard ; Karolin, Jan ; Wynne, Klaas. / Low-frequency modes of peptides and globular proteins in solution observed by ultrafast OHD-RIKES Spectroscopy. In: Biophysical Journal. 2003 ; Vol. 85, No. 3. pp. 1903-1913.
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Low-frequency modes of peptides and globular proteins in solution observed by ultrafast OHD-RIKES Spectroscopy. / Giraud, Gerard; Karolin, Jan; Wynne, Klaas.

In: Biophysical Journal, Vol. 85, No. 3, 09.2003, p. 1903-1913.

Research output: Contribution to journalArticle

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AU - Karolin, Jan

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N2 - 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.

AB - 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.

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