期刊
MOLECULES
卷 19, 期 12, 页码 19407-19434出版社
MDPI
DOI: 10.3390/molecules191219407
关键词
single molecules; conformational dynamics; single molecule FRET; free energy landscape; protein folding; allosteric regulation
资金
- People Programme (Marie Curie Actions) of the European Union [289217]
- Villum Research Centre Plant Plasticity
- Center for Synthetic Biology bioSYNergy, University of Copenhagen, Denmark
- Lundbeck foundation center of excellence Biomembranes in nanomedicine, University of Copenhagen
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.
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