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 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

Similar works

Full text



Last time updated on 12/02/2018

This paper was published in FigShare.

Having an issue?

Is data on this page outdated, violates copyrights or anything else? Report the problem now and we will take corresponding actions after reviewing your request.