What protein folding teaches us about biological function and molecular machines. (February 2015)

• Record Type: Journal Article
• Authors: Whitford, Paul C; Onuchic, José N
• Is Part Of: Current opinion in structural biology. Volume 30(2015)
• Page Start: 57
• Page End: 62
• Publication Date: 2015-02
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2014.12.003
• Languages: English
• ISSNs: 0959-440X

Abstract

Abstract : Highlights: Biomolecular folding and function are governed by a common energy landscape. Protein folding theory provides quantitative tools for describing landscapes. Order–disorder transitions are central to the function of proteins and machines. Simplified and detailed models suggest biomolecular landscapes are smooth. 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.