title: High-speed atomic force microscopy: Structure and dynamics of single proteins.
abstract: For surface analysis of biological molecules, atomic force microscopy (AFM) is an appealing technique combining data acquisition under physiological conditions, for example buffer solution, room temperature and ambient pressure, and high resolution. However, a key feature of life, dynamics, could not be assessed until recently because of the slowness of conventional AFM setups. Thus, for observing bio-molecular processes, the gain of image acquisition speed signifies a key progress. Here, we review the development and recent achievements using high-speed atomic force microscopy (HS-AFM). The HS-AFM is now the only technique to assess structure and dynamics of single molecules, revealing molecular motor action and diffusion dynamics. From this imaging data, watching molecules at work, novel and direct insights could be gained concerning the structure, dynamics and function relationship at the single bio-molecule level.
authors.affiliation: INSERM U1006, Institut Curie, 26 rue d'Ulm, 75005 Paris, France.
authors.forename: Ignacio
authors.initials: I
authors.lastname: Casuso
authors.forename: Felix
authors.initials: F
authors.lastname: Rico
authors.forename: Simon
authors.initials: S
authors.lastname: Scheuring
mesh_terms: D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D006801:Humans; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D018625:Microscopy, Atomic Force / Q000295:instrumentation / Q000379:methods*; D057054:Molecular Imaging / Q000295:instrumentation / Q000379:methods*; D020409:Molecular Motor Proteins / Q000032:analysis / Q000737:chemistry / Q000648:ultrastructure*; D013499:Surface Properties; D013816:Thermodynamics; D013997:Time Factors
chemical_list: D020409:Molecular Motor Proteins