Forster resonance energy transfer and protein-induced fluorescence enhancement as synergetic multi-scale molecular rulers.

ABSTRACT: Advanced microscopy methods allow obtaining information on (dynamic) conformational changes in biomolecules via measuring a single molecular distance in the structure. It is, however, extremely challenging to capture the full depth of a three-dimensional biochemical state, binding-related structural changes or conformational cross-talk in multi-protein complexes using one-dimensional assays. In this paper we address this fundamental problem by extending the standard molecular ruler based on Förster resonance energy transfer (FRET) into a two-dimensional assay via its combination with protein-induced fluorescence enhancement (PIFE). We show that donor brightness (via PIFE) and energy transfer efficiency (via FRET) can simultaneously report on e.g., the conformational state of double strande

SUBMITTER: Ploetz E 

PROVIDER: S-EPMC5027553 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature