title: Single-molecule fluorescence spectroscopy: new probes of protein function and dynamics.
abstract: Single-molecule fluorescence methods provide new tools for the study of biological systems. Single-pair fluorescence resonance energy transfer has provided detailed information about dynamics and structure of the Ca2+-signaling protein calmodulin. Single-molecule polarization modulation spectroscopy has probed the mechanism by which calmodulin activates the plasma membrane Ca2+ pump.
authors.affiliation: Department of Chemistry, University of Kansas, Lawrence, Kansas 66045, USA. ckjohnson@ku.edu
authors.forename: Carey K
authors.initials: CK
authors.lastname: Johnson
authors.forename: Kenneth D
authors.initials: KD
authors.lastname: Osborn
authors.forename: Michael W
authors.initials: MW
authors.lastname: Allen
authors.forename: Brian D
authors.initials: BD
authors.lastname: Slaughter
mesh_terms: D000818:Animals; D020013:Calcium Signaling; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D013050:Spectrometry, Fluorescence
chemical_list: D002147:Calmodulin; D000252:Calcium-Transporting ATPases