title: Structural dynamics of single molecules studied with high-speed atomic force microscopy.
abstract: BACKGROUND
  Atomic force microscopy (AFM) is a scanning probe technique that has been in use in biology to generate sub-nanometre resolution images in near-physiological environments for over 20 years. Most AFM work uses instruments that take several minutes to generate each image but instruments that can produce real-time images have recently become available and there is now a reasonable body of work published on this technique. The importance of this high-speed AFM is that dynamic events of individual macromolecules can be studied.
  
  
  METHODS
  This review focuses on specific examples that demonstrate the potential of the technique. It covers four areas in which high-speed AFM has been used to elucidate mechanisms that are either unstudied or not clearly understood. These areas are: protein-protein interactions; DNA-protein interactions; quantification of biological processes; the use of DNA origami scaffolds as nanostructures to build and study dynamic molecular events.
  
  
  CONCLUSIONS
  High-speed AFM shares advantages and disadvantages with conventional AFM, but it compares well in quality of data generated and in ease of use with other currently available techniques of high-resolution biological imaging. As the instruments become more widespread, the value of high-speed AFM and its potential to complement other techniques in molecular and cell biology should become more appreciated.
authors.affiliation: University of Cambridge, Department of Pharmacology , Tennis Court Road, Cambridge CB2 1PD , UK +44 1223 334053 ; rmh1003@cam.ac.uk.
authors.forename: Robert M
authors.initials: RM
authors.lastname: Henderson
mesh_terms: D004247:DNA / Q000378:metabolism; D006801:Humans; D018625:Microscopy, Atomic Force / Q000379:methods*; D056004:Molecular Dynamics Simulation; D049329:Nanostructures / Q000737:chemistry*; D011506:Proteins / Q000378:metabolism*
chemical_list: D011506:Proteins; D004247:DNA
keywords: DNA–protein interaction; atomic force microscopy; protein–protein interaction; scanning probe microscopy