title: Rotational motions of macro-molecules by single-molecule fluorescence microscopy.
abstract: Several complementary techniques have been developed to determine average orientation, dynamics on multiple time scales, and concerted rotational motions of individual fluorescent probes bound to biological macromolecules. In both protein domains and nucleic acids, tilting and wobble are relevant to their functional mechanisms. Here we briefly review methods to detect angles and rotational motions of single fluorophores and give an example of three-dimensional, total internal reflection, single-molecule fluorescence polarization applied to actin as it is translocated by conventional muscle myosin.
authors: Pennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6083, USA.
authors: Stephanie A
authors: SA
authors: Rosenberg
authors: Margot E
authors: ME
authors: Quinlan
authors: Joseph N
authors: JN
authors: Forkey
authors: Yale E
authors: YE
authors: Goldman
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D005454:Fluorescence Polarization; D005456:Fluorescent Dyes; D046911:Macromolecular Substances; D008856:Microscopy, Fluorescence / Q000379:methods*; D009218:Myosins / Q000737:chemistry / Q000378:metabolism; D012399:Rotation
chemical_list: D000199:Actins; D005456:Fluorescent Dyes; D046911:Macromolecular Substances; D009218:Myosins