@inbook{58f2e88875444f8585c4587c454c2b2a,
title = "Ensemble and single-molecule detected time-resolved FRET methods in studies of protein conformations and dynamics",
abstract = "Most proteins are nanomachines that are selected to execute specific functions and therefore should have some degree of flexibility. The driving force that excites specific motions of domains and smaller chain elements is the thermal fluctuations of the solvent bath which are channeled to selected modes of motions by the structural constraints. Consequently characterization of the ensembles of conformers of proteins and their dynamics should be expressed in statistical terms, i.e., determination of probability distributions of the various conformers. This can be achieved by measurements of time-resolved dynamic non-radiative excitation energy transfer (trFRET) within ensembles of site specifically labeled protein molecules. Distributions of intramolecular segmental end-to-end distances and their fast fluctuations can be determined, and fast and slow conformational transitions within selected sections of the molecule can be monitored and analyzed. Both ensemble and single-molecule detection methods can be applied for data collection. In combination with synchronization methods, time-resolved FRET was also used for studies of fast conformational transitions, in particular the folding/unfolding transitions.",
keywords = "Distance distributions, Fast fluctuations and conformational transitions, Intramolecular diffusion coefficient, Protein conformational dynamics, Single-molecule detection, Site-specific labeling, Time-resolved FRET",
author = "Tomer Orevi and Eitan Lerner and Gil Rahamim and Dan Amir and Elisha Haas",
year = "2014",
doi = "10.1007/978-1-62703-649-8_7",
language = "American English",
isbn = "9781627036481",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "113--169",
booktitle = "Fluorescence Spectroscopy and Microscopy",
}