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- W2023358535 abstract "Single molecule fluorescence resonance energy transfer (smFRET) was used to examine the conformational landscapes explored by the agonist binding domain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor in its apo and agonist bound forms for wild type and T686 mutant proteins. Although the average conformation for each receptor form was found to be similar to those reported by ensemble measurements, the smFRET data reveal several new points. First, the glutamate-bound form explores a wide range of conformations. The distribution of conformations was so wide as to be obscured by measurement shot-noise. By employing novel data analysis techniques, it was determined that each protein form comprised multi-state, sequential equilibria. Rate constants were extracted for the equilibrium conformational interconversions in the denoised data. These results illustrate that the extent of activation is dependent not on a rigid closed cleft, but instead on the probability that a given subunit will occupy a closed cleft conformation, which in turn is not only determined by the lowest energy state but by the range of states that the protein explores. Also, the results emphasize both the need for and the utility of advanced data processing techniques to quantify structure and dynamics in heterogeneous systems." @default.
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- W2023358535 date "2011-02-01" @default.
- W2023358535 modified "2023-09-28" @default.
- W2023358535 title "Wavelet Shrinkage to Resolve Single Molecule FRET Structural Landscape of the Isolated Ligand Binding Domain of the AMPA Receptor" @default.
- W2023358535 doi "https://doi.org/10.1016/j.bpj.2010.12.2800" @default.
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