title: Probing single-molecule protein spontaneous folding-unfolding conformational fluctuation dynamics: the multiple-state and multiple-pathway energy landscape.
abstract: Protein conformational dynamics often plays a critical role in protein functions. We have characterized the spontaneous folding-unfolding conformational fluctuation dynamics of calmodulin (CaM) at thermodynamic equilibrium conditions by using single-molecule fluorescence resonance energy transfer (FRET) spectroscopy. We have identified multiple folding transition pathways and characterized the underlying energy landscape of the single-molecule protein conformational fluctuation trajectories, using a model analysis based on the detailed balance rate process principle. Our results suggest that the folding dynamics of CaM molecules involves a complex multiple-pathway multiple-state energy landscape, rather than an energy landscape of two-state dynamical process. Our probing single-molecule FRET fluctuation experiments demonstrate a new approach of studying spontaneous protein folding-unfolding conformational dynamics at the equilibrium that features recording long time single-molecule conformational fluctuation trajectories.
authors: Center for Photochemical Sciences, Department of Chemistry, Bowling Green State University, Bowling Green, Ohio 43403, United States.
authors: Zijian
authors: Z
authors: Wang
authors: Center for Photochemical Sciences, Department of Chemistry, Bowling Green State University, Bowling Green, Ohio 43403, United States.
authors: H Peter
authors: HP
authors: Lu
mesh_terms: D002147:Calmodulin / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D002147:Calmodulin