Bulletin of the Chemical Society of Japan
Online ISSN : 1348-0634
Print ISSN : 0009-2673
ISSN-L : 0009-2673
The Chemical Society of Japan Award for Creative Work for 2012
Time-Resolved Resonance Raman Spectroscopy and Application to Studies on Ultrafast Protein Dynamics
Yasuhisa Mizutani
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2017 Volume 90 Issue 12 Pages 1344-1371


Protein dynamics play a fundamental role in allosteric regulation, which is vital to the function of many proteins. In many proteins, rather than a direct interaction, mutual modulation of properties such as ligand affinity at spatially separated sites is achieved through a conformational change. Conformational changes of proteins are thermally activated processes that involve intramolecular and intermolecular energy exchanges. In this account, I review the work of my team on the development and applications of ultrafast time-resolved resonance Raman spectroscopy to observe functionally important protein dynamics. We gained insights into conformational dynamics upon external stimulus and energy flow with a spatial resolution of a single amino acid residue using time-resolved visible and ultraviolet resonance Raman spectroscopy. The results have contributed to a deeper understanding of the structural nature of protein motion and the relationship of dynamics to function. I discuss the protein dynamics and allosteric mechanism in terms of the nature of the high packing density of protein structures. In addition, I present a view of the future of molecular science on proteins.

Time-resolved visible and ultraviolet resonance Raman spectroscopy were used to determine conformational dynamics upon an external stimulus and energy flow with a spatial resolution of a single amino acid residue in proteins. This account summarizes the accomplishments that promoted an understanding of how proteins change structure to realize their functions and how energy dissipation is coupled to protein structure and dynamics. Fullsize Image
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© 2017 The Chemical Society of Japan
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