Structural and dynamic characterization of biochemical processes by atomic force microscopy

Frédéric Eghiaian, Iwan a T Schaap

Research output: Chapter in Book/Report/Conference proceedingChapter

9 Citations (Scopus)


Atomic Force Microscopy (AFM) has gained increasing popularity over the years among biophysicists due to its ability to image and to measure pN to nN forces on biologically relevant scales (nm to μm). Continuous technical developments have made AFM capable of nondisruptive, subsecond imaging of fragile biological samples in a liquid environment, making this method a potent alternative to light microscopy. In this chapter, we discuss the basics of AFM, its theoretical limitations, and we describe how this technique can be used to get single protein resolution in liquids at room temperature. Provided imaging is done at low-enough forces to avoid sample disruption and conformational changes, AFM allows obtaining unique insights into enzyme dynamics.
Original languageEnglish
Title of host publicationSingle Molecule Enzymology
Subtitle of host publicationMethods and Protocols
PublisherHumana Press
Number of pages25
ISBN (Electronic)978-1-61779-261-8
ISBN (Print)978-1-61779-260-1
Publication statusPublished - 2011

Publication series

NameMethods in molecular biology (Clifton, N.J.)
PublisherHumana Press
ISSN (Print)1064-3745


  • afm
  • atomic force microscopy
  • cantilever
  • kinesin
  • microtubule
  • silane
  • thermal noise
  • virus


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