Abstract
Forster resonance energy transfer (FRET) is a powerful tool for studying biological systems at the nanometer length-scale. Further, FRET is used to probe the conformational dynamics of single biomolecules with Angstrom-scale precision. Such studies require that an appropriate fluorophore pair is tethered to the molecule of interest, most often through site-mutations to accommodate specific fluorophore linker chemistry. This approach is at its most powerful when separate experiments with different labeling sites, constituting a FRET network, are considered simultaneously as complementary restraints in determining the conformational states of the molecule.
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