title: Muscle, myosin and single molecules.
abstract: Whereas we have a great deal of information about myosin, there remain fundamental questions about its mechanism (and those of other motor proteins). Single-molecule technologies enable us to make measurements we cannot make from large ensembles of molecules. Optical tweezers (and similar techniques) are used to measure the mechanical aspects of actomyosin interactions, including force, displacement and stiffness. Single-molecule fluorescence has been used to observe the binding and release of nucleotide by myosins. A combination of these measurements has the potential to solve the problem of coupling of ATP hydrolysis to mechanical work in motor proteins.
authors.affiliation: Biology Department, University of York, P.O. Box 373, York YO10 5YW, U.K.
authors.forename: A E
authors.initials: AE
authors.lastname: Knight
authors.forename: J E
authors.initials: JE
authors.lastname: Molloy
mesh_terms: D000199:Actins / Q000378:metabolism; D000205:Actomyosin / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D006801:Humans; D020409:Molecular Motor Proteins / Q000502:physiology*; D009119:Muscle Contraction / Q000502:physiology; D009132:Muscles / Q000502:physiology*; D009218:Myosins / Q000378:metabolism*
chemical_list: D000199:Actins; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D000205:Actomyosin; D009218:Myosins