화학공학소재연구정보센터
Journal of Physical Chemistry B, Vol.119, No.21, 6366-6378, 2015
Probing Single-Molecule Protein Spontaneous Folding-Unfolding Conformational Fluctuation Dynamics: The Multiple-State and Multiple-Pathway Energy Landscape
Protein conformational dynamics often plays a critical role in protein. functions We have Chatacterized 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.