title: Single-molecule folding.
abstract: Recent developments in fluorescence and force spectroscopy enable us to go beyond the ensemble average and measure the behavior of individual biomacromolecules. These single-molecule approaches can directly resolve transient intermediate states and multiple reaction pathways, and thus are uniquely powerful in characterizing the complex dynamics of biological processes. Recent applications of these two techniques to the protein and RNA folding problems have led to exciting new results.
authors.affiliation: Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA. zhuang@chemistry.harvard.edu
authors.forename: Xiaowei
authors.initials: X
authors.lastname: Zhuang
authors.forename: Matthias
authors.initials: M
authors.lastname: Rief
mesh_terms: D064211:Connectin; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D046911:Macromolecular Substances; D018625:Microscopy, Atomic Force / Q000379:methods*; D008958:Models, Molecular; D009038:Motion; D009124:Muscle Proteins / Q000737:chemistry; D009690:Nucleic Acid Conformation; D010812:Physical Stimulation / Q000379:methods; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012313:RNA / Q000737:chemistry*
chemical_list: D064211:Connectin; D046911:Macromolecular Substances; D009124:Muscle Proteins; D011506:Proteins; D012313:RNA; D011494:Protein Kinases