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Shedding Light on Protein Folding, Structural and Functional Dynamics by Single Molecule Studies

1
Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Center for Synthetic Biology "bioSYNergy", Villum Research Center "Plant Plasticity", University of Copenhagen, Thorvaldsenvej 40, DK-1871 Frederiksberg C, Denmark
2
Bio-Nanotechnology Laboratory, Department of Chemistry, Nano-Science Center, Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, 2100 Copenhagen, Denmark
*
Author to whom correspondence should be addressed.
Molecules 2014, 19(12), 19407-19434; https://doi.org/10.3390/molecules191219407
Received: 30 July 2014 / Revised: 7 November 2014 / Accepted: 12 November 2014 / Published: 25 November 2014
(This article belongs to the Special Issue Single Molecule Techniques)
The advent of advanced single molecule measurements unveiled a great wealth of dynamic information revolutionizing our understanding of protein dynamics and behavior in ways unattainable by conventional bulk assays. Equipped with the ability to record distribution of behaviors rather than the mean property of a population, single molecule measurements offer observation and quantification of the abundance, lifetime and function of multiple protein states. They also permit the direct observation of the transient and rarely populated intermediates in the energy landscape that are typically averaged out in non-synchronized ensemble measurements. Single molecule studies have thus provided novel insights about how the dynamic sampling of the free energy landscape dictates all aspects of protein behavior; from its folding to function. Here we will survey some of the state of the art contributions in deciphering mechanisms that underlie protein folding, structural and functional dynamics by single molecule fluorescence microscopy techniques. We will discuss a few selected examples highlighting the power of the emerging techniques and finally discuss the future improvements and directions. View Full-Text
Keywords: single molecules; conformational dynamics; single molecule FRET; free energy landscape; protein folding; allosteric regulation single molecules; conformational dynamics; single molecule FRET; free energy landscape; protein folding; allosteric regulation
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Bavishi, K.; Hatzakis, N.S. Shedding Light on Protein Folding, Structural and Functional Dynamics by Single Molecule Studies. Molecules 2014, 19, 19407-19434.

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