Time-Resolved Optical Kerr-Effect Spectroscopy of Low-Frequency Dynamics in Di-l-alanine, Poly-l-alanine, and Lysozyme in Solution

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 thos...

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Published inJournal of the American Chemical Society Vol. 124; no. 41; pp. 12110 - 12111
Main Authors Giraud, Gerard, Wynne, Klaas
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 16.10.2002
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Summary: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 α-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 α-helix. The mostly α-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.
Bibliography:ark:/67375/TPS-K1C0BJ51-B
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ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0002-7863
1520-5126
DOI:10.1021/ja027801h