title: What protein folding teaches us about biological function and molecular machines.
abstract: Protein folding was the first area of molecular biology for which a systematic statistical-mechanical analysis of dynamics was developed. As a result, folding is described as a process by which a disordered protein chain diffuses across a high-dimensional energy landscape and finally reaches the folded ensemble. Folding studies have produced countless theoretical concepts that are generalizable to other biomolecular processes, such as the functional dynamics of molecular assemblies. Common themes in folding and function include the dominant role of excluded volume, that a balance between energetic roughness and geometrical effects guides dynamics, and that folding/functional landscapes are relatively smooth. Here, we discuss how insights into protein folding have been applied to investigate the functional dynamics of biomolecular assemblies.
authors.affiliation: Department of Physics, Northeastern University, 360 Huntington Avenue, Boston, MA 02115, United States. Electronic address: p.whitford@neu.edu.
authors.forename: Paul C
authors.initials: PC
authors.lastname: Whitford
authors.affiliation: Center for Theoretical Biological Physics, Rice University, Houston, TX 77251, United States. Electronic address: jonuchic@rice.edu.
authors.forename: José N
authors.initials: JN
authors.lastname: Onuchic
mesh_terms: D004058:Diffusion; D046911:Macromolecular Substances / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D017510:Protein Folding
chemical_list: D046911:Macromolecular Substances