Abstract
Various ways of extracting information on the conformational structure, dynamics and correlations between them from single-molecule measurements of orescence resonance energy transfer are surveyed. The information obtained via those various ways is then analyzed in detail in the case of an off-lattice model of a two-stranded coiled-coil polypeptide that follows Langevin dynamics. The analysis includes a consideration of the cases of a freely diffusing and surface-immobilized polypeptide as well as the effect of different types of surface and denaturation conditions.
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Geva, E., Shang, J. (2009). Conformational Structure and Dynamics from Single-Molecule FRET. In: Burghardt, I., May, V., Micha, D., Bittner, E. (eds) Energy Transfer Dynamics in Biomaterial Systems. Springer Series in Chemical Physics, vol 93. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-02306-4_3
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