title: Understanding disordered and unfolded proteins using single-molecule FRET and polymer theory.
abstract: Understanding protein folding and the functional properties of intrinsically disordered proteins (IDPs) requires detailed knowledge of the forces that act in polypeptide chains. These forces determine the dimensions and dynamics of unfolded and disordered proteins and have been suggested to impact processes such as the coupled binding and folding of IDPs, or the rate of protein folding reactions. Much of the progress in understanding the physical and chemical properties of unfolded and intrinsically disordered polypeptide chains has been made possible by the recent developments in single-molecule fluorescence techniques. However, the interpretation of the experimental results requires concepts from polymer physics in order to be understood. Here, I review some of the theories used to describe the dimensions of unfolded polypeptide chains under varying solvent conditions together with their more recent application to experimental data.
authors.affiliation: Department of Structural Biology, Weizmann Institute of Science, Herzl St. 234, 76100 Rehovot, Israel.
authors.forename: Hagen
authors.initials: H
authors.lastname: Hofmann
mesh_terms: D031541:Fluorescence Resonance Energy Transfer; D064267:Intrinsically Disordered Proteins; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D011108:Polymers; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D064267:Intrinsically Disordered Proteins; D011108:Polymers