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.
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