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Published on Web Date: February 17, 2011 r 2011 American Chemical Society 334 DOI: 10.1021/jz101619f |J. Phys. Chem. Lett. 2011, 2, 334344
 

Summary: Published on Web Date: February 17, 2011
r 2011 American Chemical Society 334 DOI: 10.1021/jz101619f |J. Phys. Chem. Lett. 2011, 2, 334344
PERSPECTIVE
pubs.acs.org/JPCL
Elucidating Peptide and Protein Structure and Dynamics:
UV Resonance Raman Spectroscopy
Sulayman A. Oladepo, Kan Xiong, Zhenmin Hong, and Sanford A. Asher*
Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States
ABSTRACT UV resonance Raman spectroscopy (UVRR) is a powerful method
that has the requisite selectivity and sensitivity to incisively monitor biomolecular
structure and dynamics in solution. In this Perspective, we highlight applications of
UVRR for studying peptide and protein structure and the dynamics of protein and
peptide folding. UVRR spectral monitors of protein secondary structure, such as
the amide III3 band and the CR;H band frequencies and intensities, can be used to
determine Ramachandran angle distributions for peptide bonds. These incisive,
quantitative glimpses into conformation can be combined with kinetic T-jump
methodologies to monitor the dynamics of biomolecular conformational transi-
tions. The resulting UVRR structural insight is impressive in that it allows differ-
entiation of, for example, different R-helix-like states that enable differentiating
and 310 states from pure R-helices. These approaches can be used to determine the

  

Source: Asher, Sanford A. - Department of Chemistry, University of Pittsburgh

 

Collections: Materials Science; Chemistry