title: Application of confocal single-molecule FRET to intrinsically disordered proteins.
abstract: Intrinsically disordered proteins (IDPs) are characterized by a large degree of conformational heterogeneity. In such cases, classical experimental methods often yield only mean values, averaged over the entire ensemble of molecules. The microscopic distributions of conformations, trajectories, or sequences of events often remain unknown, and with them the underlying molecular mechanisms. Signal averaging can be avoided by observing individual molecules. A particularly versatile method is highly sensitive fluorescence detection. In combination with Förster resonance energy transfer (FRET), distances and conformational dynamics can be investigated in single molecules. This chapter introduces the practical aspects of applying confocal single-molecule FRET experiments to the study of IDPs.
authors: Department of Biochemistry, University of Zurich, Zurich, Switzerland. schuler@bioc.uzh.ch
authors: Benjamin
authors: B
authors: Schuler
authors: Sonja
authors: S
authors: Müller-Späth
authors: Andrea
authors: A
authors: Soranno
authors: Daniel
authors: D
authors: Nettels
mesh_terms: D004058:Diffusion; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D005456:Fluorescent Dyes / Q000737:chemistry; D055767:Immobilized Proteins / Q000737:chemistry*; D008958:Models, Molecular; D055620:Optical Phenomena; D017785:Photons; D011487:Protein Conformation; D058767:Protein Unfolding; D013194:Staining and Labeling; D013997:Time Factors
chemical_list: D005456:Fluorescent Dyes; D055767:Immobilized Proteins