title: Ensemble FRET methods in studies of intrinsically disordered proteins.
abstract: The main structural characteristic of intrinsically disordered proteins (IDPs) or intrinsically disordered regions of globular proteins is that they exist as ensembles of multiple conformers which can continuously interconvert, and at times, form ensembles of a more restricted number of conformers. Characterization of the disordered state and transitions to partially or fully ordered states of such ensembles must be expressed in statistical terms, i.e., determination of probability distributions of the various conformers. This can be achieved by measurements of time-resolved dynamic non-radiative excitation energy transfer within ensembles of site-specifically labeled IDP molecules. Distributions of intramolecular segmental end-to-end distances and their fast fluctuations can be determined and fast and slow conformational transitions within selected sections of the molecule can be monitored and analyzed.
authors: The Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel. Elisha.haas@biu.ac.il
authors: Elisha
authors: E
authors: Haas
mesh_terms: D000465:Algorithms; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D011487:Protein Conformation; D011789:Quantum Theory; D013194:Staining and Labeling; D051844:alpha-Synuclein / Q000737:chemistry*
chemical_list: D016229:Amyloid beta-Peptides; D051844:alpha-Synuclein