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- W2038049470 abstract "One of the most abundant proteins in eukaryotes is actin, a ubiquitous protein that plays a role in cell dynamics like cell migration. The dynamics of actin filament treadmilling is regulated by two actin structural states: globular actin (G-actin) and filamentous actin (F-actin). While G-actin's crystal structure has been solved by several groups, F-actin's has not. Although recently it was reported that the structure for the two actins differ (Oda et al), there is still much to resolve on the matter of their dynamic structures. Here we observed the dynamics of the actin structural states under various conditions by using single-molecule FRET in combination with total internal reflection fluorescence microscopy. To conduct these experiments, we first labeled actin residues 41 and 374, having substituted Gln 41 with Cys. The new Cys 41 site along with Cys 374 were used for site-directed labeling by SH-group reactive fluorescent dyes. We found that F-actin has at least two distinct states, and that the population distribution of these states was dependent on the ionic conditions. We are currently investigating these states by performing FRET measurements for observing the long -time transition between the two states." @default.
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- W2038049470 date "2010-01-01" @default.
- W2038049470 modified "2023-09-30" @default.
- W2038049470 title "Multiple Structural Forms of Actin in the Filamentous State" @default.
- W2038049470 doi "https://doi.org/10.1016/j.bpj.2009.12.827" @default.
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