title: Probing the structural dynamics of proteins and nucleic acids with optical tweezers.
abstract: Conformational changes are an essential feature of most molecular processes in biology. Optical tweezers have emerged as a powerful tool for probing conformational dynamics at the single-molecule level because of their high resolution and sensitivity, opening new windows on phenomena ranging from folding and ligand binding to enzyme function, molecular machines, and protein aggregation. By measuring conformational changes induced in a molecule by forces applied by optical tweezers, new insight has been gained into the relationship between dynamics and function. We discuss recent advances from studies of how structure forms in proteins and RNA, including non-native structures, fluctuations in disordered proteins, and interactions with chaperones assisting native folding. We also review the development of assays probing the dynamics of complex protein-nucleic acid and protein-protein assemblies that reveal the dynamic interactions between biomolecular machines and their substrates.
authors.affiliation: Department of Physics, University of Alberta, Edmonton, AB T6G2E1 Canada.
authors.forename: Dustin B
authors.initials: DB
authors.lastname: Ritchie
authors.affiliation: Department of Physics, University of Alberta, Edmonton, AB T6G2E1 Canada; National Institute for Nanotechnology, National Research Council, Edmonton, AB T6G2M9, Canada. Electronic address: Michael.Woodside@ualberta.ca.
authors.forename: Michael T
authors.initials: MT
authors.lastname: Woodside
mesh_terms: D064267:Intrinsically Disordered Proteins / Q000737:chemistry; D008958:Models, Molecular; D008968:Molecular Conformation; D009690:Nucleic Acid Conformation; D009696:Nucleic Acids / Q000737:chemistry* / Q000378:metabolism; D052898:Optical Tweezers; D066263:Protein Aggregation, Pathological; D017510:Protein Folding; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D064267:Intrinsically Disordered Proteins; D009696:Nucleic Acids; D011506:Proteins; D012313:RNA