Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET.

ABSTRACT: Proteins are the workhorses of biology, orchestrating a myriad of cellular functions through intricate conformational changes. Protein allostery, the phenomenon where binding of ligands or environmental changes induce conformational rearrangements in the protein, is fundamental to these processes. We have previously shown that transition metal Förster resonance energy transfer (tmFRET) can be used to interrogate the conformational rearrangements associated with protein allostery and have recently introduced novel FRET acceptors utilizing metal-bipyridyl derivatives to measure long (>20 Å) intramolecular distances in proteins. Here, we combine our tmFRET system with fluorescence lifetime measurements to measure the distances, conformational heterogeneity, and energetics of maltose binding p

SUBMITTER: Zagotta WN 

PROVIDER: S-EPMC10592786 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature