Single-Molecule FRET Spectroscopy and the Polymer Physics of Unfolded and Intrinsically Disordered Proteins
- 5 July 2016
- journal article
- review article
- Published by Annual Reviews in Annual Review of Biophysics
- Vol. 45 (1), 207-231
- https://doi.org/10.1146/annurev-biophys-062215-010915
Abstract
The properties of unfolded proteins have long been of interest because of their importance to the protein folding process. Recently, the surprising prevalence of unstructured regions or entirely disordered proteins under physiological conditions has led to the realization that such intrinsically disordered proteins can be functional even in the absence of a folded structure. However, owing to their broad conformational distributions, many of the properties of unstructured proteins are difficult to describe with the established concepts of structural biology. We have thus seen a reemergence of polymer physics as a versatile framework for understanding their structure and dynamics. An important driving force for these developments has been single-molecule spectroscopy, as it allows structural heterogeneity, intramolecular distance distributions, and dynamics to be quantified over a wide range of timescales and solution conditions. Polymer concepts provide an important basis for relating the physical propert...Keywords
This publication has 178 references indexed in Scilit:
- Small-Angle X-ray Scattering and Single-Molecule FRET Spectroscopy Produce Highly Divergent Views of the Low-Denaturant Unfolded StateJournal of Molecular Biology, 2012
- How, when and why proteins collapse: the relation to foldingCurrent Opinion in Structural Biology, 2012
- Single Molecule Study of the Intrinsically Disordered FG-Repeat Nucleoporin 153Biophysical Journal, 2011
- Beyond the Random Coil: Stochastic Conformational Switching in Intrinsically Disordered ProteinsStructure, 2011
- Effects of Macromolecular Crowding on an Intrinsically Disordered Protein Characterized by Small-Angle Neutron Scattering with Contrast MatchingBiophysical Journal, 2011
- Fluorescence Correlation Spectroscopy of Fast Chain Dynamics within Denatured Protein LChemphyschem, 2011
- Dependence of Protein Folding Stability and Dynamics on the Density and Composition of Macromolecular CrowdersBiophysical Journal, 2010
- Linking folding and bindingCurrent Opinion in Structural Biology, 2009
- Fluorescence characterization of denatured proteinsCurrent Opinion in Structural Biology, 2008
- ABSINTH: A new continuum solvation model for simulations of polypeptides in aqueous solutionsJournal of Computational Chemistry, 2008