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• W252082922 abstract "The experimental study of individual macromolecules has opened a door to determining the details of their mechanochemical operation. Motor enzymes such as the myosin family have been particularly attractive targets for such study, in part because some of them are highly processive and their product is spatial motion. But single-molecule resolution comes with its own costs and limitations. Often, the observations rest on single fluorescent dye molecules, which emit a limited number of photons before photobleaching and are subject to complex internal dynamics. Thus, it is important to develop methods that extract the maximum useful information from a finite set of detected photons. We have extended an experimental technique, multiple polarization illumination in total internal reflection fluorescence microscopy (polTIRF), to record the arrival time and polarization state of each individual detected photon. We also extended an analysis technique, previously applied to FRET experiments, that optimally determines times of changes in photon emission rates. Combining these improvements allows us to identify the structural dynamics of a molecular motor (myosin V) with unprecedented detail and temporal resolution." @default.
• W252082922 created "2016-06-24" @default.
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• W252082922 creator A5065112291 @default.
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• W252082922 date "2011-01-01" @default.
• W252082922 modified "2023-09-30" @default.
• W252082922 title "Changepoint Analysis for Single-Molecule Polarized Total Internal Reflection Fluorescence Microscopy Experiments" @default.
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• W252082922 doi "https://doi.org/10.1016/b978-0-12-381270-4.00015-9" @default.
• W252082922 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3142583" @default.
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• W252082922 hasPublicationYear "2011" @default.
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