title: Single-molecule protein interaction conformational dynamics.
abstract: Protein conformational fluctuations and dynamics, often associated with static and dynamic inhomogeneities, play a crucial role in biomolecular functions. It is extremely difficult to characterize such spatially and temporally inhomogeneous dynamics in an ensemble-averaged measurement, especially when the proteins involve in a multiple-step and multiple-conformation complex chemical interactions and transformations, such as in protein-protein interactions and protein-DNA interactions. Single-molecule spectroscopy is a powerful approach to analyze protein conformational dynamics under physiological conditions, providing dynamic perspectives on a molecular-level understanding of protein structure-function mechanisms.
authors.affiliation: Department of Chemistry, Center for Photochemical Sciences, Bowling Green State University, Bowling Green, OH 43403, USA. hplu@bgsu.edu
authors.forename: H Peter
authors.initials: HP
authors.lastname: Lu
mesh_terms: D000465:Algorithms; D002147:Calmodulin / Q000737:chemistry; D002450:Cell Communication; D004247:DNA / Q000737:chemistry; D004249:DNA Damage; D031541:Fluorescence Resonance Energy Transfer; D011487:Protein Conformation; D015398:Signal Transduction; D013050:Spectrometry, Fluorescence
chemical_list: D002147:Calmodulin; D004247:DNA