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UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics

Authors :
Joseph Handen
Sulayman A. Oladepo
Igor K. Lednev
Zhenmin Hong
Sanford A. Asher
Kan Xiong
Source :
Chemical Reviews. 112:2604-2628
Publication Year :
2012
Publisher :
American Chemical Society (ACS), 2012.

Abstract

A study was conducted to demonstrate ultraviolet resonance Raman (UVRR) investigations of peptide and protein structure and dynamics. The tuning of the excitation wavelengths allowed the probing of different chromophoric segments of a macromolecule. Another advantage of deep UV Raman measurements was that there was no interference from molecular relaxed fluorescence, as those chromophores that had their first transition below 260 nm were highly flexible and possessed small fluorescence quantum yields. UVRR was also used in pump-probe measurements to give kinetic information on fast biological processes. It was a powerful technique for studying static protein structure and for studying protein dynamics, such as in protein folding. The rapid development of UVRR was aided by the latest advancements in lasers, optics, and detectors.

Details

ISSN :
15206890 and 00092665
Volume :
112
Database :
OpenAIRE
Journal :
Chemical Reviews
Accession number :
edsair.doi.dedup.....95c26f5e842b602969912c0149fc8d60