Time-resolved optical Kerr-effect spectroscopy of low-frequency dynamics in Di-L-alanine, poly-L-alanine, and lysozyme in solution

Gerard Giraud, Klaas Wynne

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

The low-frequency spectra of peptides and proteins in solution have been investigated with optical heterodyne-detected Raman-induced Kerr-effect spectroscopy. Spectra were obtained for di-L-alanine ALA(2) and poly-L-alanine (PLA) in dichloroacetic acid solution. The conformational dependence of those spectra at low frequency has been analyzed. ALA(2) displays a band centered at 50 cm-1, whereas the -helical PLA shows two shoulders at 60 and 140 cm-1. The similarity of the spectral features observed in PLA to those in water can be explained by analogous acoustic translational modes in the hydrogen network of the PLA -helix. The mostly -helical protein lysozyme in aqueous solution has also been investigated and showed significantly more structure with modes at 10, 35, 73, 106, and 164 cm-1.
LanguageEnglish
Pages12110-12111
Number of pages1
JournalJournal of Chemical Physics
Volume124
Issue number41
DOIs
Publication statusPublished - 21 Sep 2002

Fingerprint

Optical Kerr effect
lysozyme
alanine
Muramidase
Kerr effects
Spectroscopy
low frequencies
spectroscopy
Dichloroacetic Acid
proteins
Alanine
Hydrogen
shoulders
Proteins
helices
peptides
Peptides
polyalanine
Water
aqueous solutions

Keywords

  • Kerr-effect spectroscopy
  • low-frequency dynamics
  • Di-L-alanine
  • poly-L-alanine
  • lysozyme
  • nanoscience

Cite this

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title = "Time-resolved optical Kerr-effect spectroscopy of low-frequency dynamics in Di-L-alanine, poly-L-alanine, and lysozyme in solution",
abstract = "The low-frequency spectra of peptides and proteins in solution have been investigated with optical heterodyne-detected Raman-induced Kerr-effect spectroscopy. Spectra were obtained for di-L-alanine ALA(2) and poly-L-alanine (PLA) in dichloroacetic acid solution. The conformational dependence of those spectra at low frequency has been analyzed. ALA(2) displays a band centered at 50 cm-1, whereas the -helical PLA shows two shoulders at 60 and 140 cm-1. The similarity of the spectral features observed in PLA to those in water can be explained by analogous acoustic translational modes in the hydrogen network of the PLA -helix. The mostly -helical protein lysozyme in aqueous solution has also been investigated and showed significantly more structure with modes at 10, 35, 73, 106, and 164 cm-1.",
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Time-resolved optical Kerr-effect spectroscopy of low-frequency dynamics in Di-L-alanine, poly-L-alanine, and lysozyme in solution. / Giraud, Gerard; Wynne, Klaas.

In: Journal of Chemical Physics, Vol. 124, No. 41, 21.09.2002, p. 12110-12111.

Research output: Contribution to journalArticle

TY - JOUR

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AU - Wynne, Klaas

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AB - The low-frequency spectra of peptides and proteins in solution have been investigated with optical heterodyne-detected Raman-induced Kerr-effect spectroscopy. Spectra were obtained for di-L-alanine ALA(2) and poly-L-alanine (PLA) in dichloroacetic acid solution. The conformational dependence of those spectra at low frequency has been analyzed. ALA(2) displays a band centered at 50 cm-1, whereas the -helical PLA shows two shoulders at 60 and 140 cm-1. The similarity of the spectral features observed in PLA to those in water can be explained by analogous acoustic translational modes in the hydrogen network of the PLA -helix. The mostly -helical protein lysozyme in aqueous solution has also been investigated and showed significantly more structure with modes at 10, 35, 73, 106, and 164 cm-1.

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KW - low-frequency dynamics

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KW - poly-L-alanine

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