title: Functional surface attachment in a sandwich geometry of GFP-labeled motor proteins.
abstract: Molecular motors perform work in cells by moving in an ATP-dependent manner along filamentous tracks. In vitro, the mechanical action of such motor proteins can be investigated by attaching the molecules to surfaces in the so-called gliding or bead assays. Surface attachment protocols have to be used that do not interfere with the function of the molecule. Here, we describe a sandwich protocol that preserves functionality. The protocol can be used for a large variety of proteins, in particular kinesin motor proteins that are GFP-tagged.
authors.affiliation: Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
authors.forename: Volker
authors.initials: V
authors.lastname: Bormuth
authors.forename: Felix
authors.initials: F
authors.lastname: Zörgibel
authors.forename: Erik
authors.initials: E
authors.lastname: Schäffer
authors.forename: Jonathon
authors.initials: J
authors.lastname: Howard
mesh_terms: D001696:Biomechanical Phenomena; D049452:Green Fluorescent Proteins / Q000737:chemistry*; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D020409:Molecular Motor Proteins; D049452:Green Fluorescent Proteins; D016547:Kinesins