High-speed atomic force microscopy: Structure and dynamics of single proteins

Curr Opin Chem Biol. 2011 Oct;15(5):704-9. doi: 10.1016/j.cbpa.2011.05.007. Epub 2011 May 31.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure*
  • Humans
  • Image Processing, Computer-Assisted / methods*
  • Microscopy, Atomic Force / instrumentation
  • Microscopy, Atomic Force / methods*
  • Molecular Imaging / instrumentation
  • Molecular Imaging / methods*
  • Molecular Motor Proteins / analysis
  • Molecular Motor Proteins / chemistry
  • Molecular Motor Proteins / ultrastructure*
  • Surface Properties
  • Thermodynamics
  • Time Factors

Substances

  • Molecular Motor Proteins