Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy

作者：Oladepo Sulayman A; Xiong Kan; Hong Zhenmin; Asher Sanford A^*

来源：Journal of Physical Chemistry Letters, 2011, 2(4): 334-344.

DOI：10.1021/jz101619f

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 III(3) band and the C(alpha)-H band frequencies and intensities, can be used to determine Ramachandran Psi 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 transitions. The resulting UVRR structural insight is impressive in that it allows differentiation of, for example, different alpha-helix-like states that enable differentiating pi and 3(10), states from pure alpha-helices. These approaches can be used to determine the Gibbs free energy landscape of individual peptide bonds along the most important protein (un)folding coordinate. Future work will find spectral monitors that probe peptide bond activation barriers that control protein (un)folding mechanisms, In addition, UVRR studies of side chain vibrations will probe the role of side chains in determining protein secondary tertiary and quaternary structures.

• 出版日期2011-2-17