title: Kinesin motion in the absence of external forces characterized by interference total internal reflection microscopy.
abstract: We study the motion of the kinesin molecular motor along microtubules using interference total internal reflection microscopy. This technique achieves nanometer scale resolution together with a fast time response. We describe the first in vitro observation of kinesin stepping at high ATP concentration in the absence of an external load, where the 8-nm step can be clearly distinguished. The short-time resolution allows us to measure the time constant related to the relative motion of the bead-motor connection; we deduce the associated bead-motor elastic modulus.
authors.affiliation: Physico Chimie Curie, UMR CNRS/IC 168, 26 rue d'Ulm, 75248 Paris Cedex 05, France. Giovanni.Cappello@Curie.fr
authors.forename: Giovanni
authors.initials: G
authors.lastname: Cappello
authors.forename: Mathilde
authors.initials: M
authors.lastname: Badoual
authors.forename: Albrecht
authors.initials: A
authors.lastname: Ott
authors.forename: Jacques
authors.initials: J
authors.lastname: Prost
authors.forename: Lorenzo
authors.initials: L
authors.lastname: Busoni
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D055592:Biophysical Phenomena; D001703:Biophysics; D019921:Biotinylation; D006868:Hydrolysis; D016547:Kinesins / Q000737:chemistry*; D008857:Microscopy, Interference / Q000295:instrumentation / Q000379:methods; D020409:Molecular Motor Proteins; D009492:Neurospora crassa / Q000378:metabolism; D013997:Time Factors
chemical_list: D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D016547:Kinesins