Work

UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics

Year: 2012

Type: review

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.

Source: Chemical Reviews

DOI: 10.1021/cr200198a

Authors: Sulayman A. Oladepo, Kan Xiong, Zhenmin Hong, Sanford A. Asher, Joseph Handen, Igor K. Lednev

Institutions: University of Pittsburgh, University at Albany, State University of New York

Language: English

Topic: Spectroscopy Techniques in Biomedical and Chemical Research

Subfield: Biophysics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institute on Aging, National Institute of Biomedical Imaging and Bioengineering

Awards: Ultrahigh Throughput Deep UV Raman Spectrometer for Probing Protein Structure, Structural Characterization of Amyloid Fibrils Using Deep UV Raman Spectroscopy