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Deciphering hierarchical features in the energy landscape of adenylate kinase folding/unfolding

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Title: Deciphering hierarchical features in the energy landscape of adenylate kinase folding/unfolding
Authors: Taylor, J. Nicholas Browse this author
Pirchi, Menahem Browse this author
Haran, Gilad Browse this author
Komatsuzaki, Tamiki Browse this author →KAKEN DB
Issue Date: 28-Mar-2018
Publisher: American Institute of Physics (AIP)
Journal Title: Journal of chemical physics
Volume: 148
Issue: 12
Start Page: 123325
Publisher DOI: 10.1063/1.5016487
Abstract: Hierarchical features of the energy landscape of the folding/unfolding behavior of adenylate kinase, including its dependence on denaturant concentration, are elucidated in terms of single-molecule fluorescence resonance energy transfer (smFRET) measurements in which the proteins are encapsulated in a lipid vesicle. The core in constructing the energy landscape from single-molecule time-series across different denaturant concentrations is the application of rate-distortion theory (RDT), which naturally considers the effects of measurement noise and sampling error, in combination with change-point detection and the quantification of the FRET efficiency-dependent photobleaching behavior. Energy landscapes are constructed as a function of observation time scale, revealing multiple partially folded conformations at small time scales that are situated in a superbasin. As the time scale increases, these denatured states merge into a single basin, demonstrating the coarse-graining of the energy landscape as observation time increases. Because the photobleaching time scale is dependent on the conformational state of the protein, possible nonequilibrium features are discussed, and a statistical test for violation of the detailed balance condition is developed based on the state sequences arising from the RDT framework. Published by AIP Publishing.
Rights: The following article appeared in J. Nicholas Taylor, Menahem Pirchi, Gilad Haran, and Tamiki Komatsuzaki. Deciphering hierarchical features in the energy landscape of adenylate kinase folding/unfolding. The Journal of Chemical Physics 148, 123325 (2018) and may be found at https://doi.org/10.1063/1.5016487 .
Type: article
URI: http://hdl.handle.net/2115/73333
Appears in Collections:電子科学研究所 (Research Institute for Electronic Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: James Nicholas TAYLOR

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