Skip to Main content Skip to Navigation
Journal articles

High-speed atomic force microscopy: Structure and dynamics of single proteins This review comes from a themed issue on Analytical Techniques Edited

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.
Document type :
Journal articles
Complete list of metadatas

Cited literature [42 references]  Display  Hide  Download

https://www.hal.inserm.fr/inserm-01363295
Contributor : U1006 Aix-Marseille Université <>
Submitted on : Friday, September 9, 2016 - 3:18:27 PM
Last modification on : Thursday, May 17, 2018 - 5:18:01 PM
Long-term archiving on: : Saturday, December 10, 2016 - 1:13:17 PM

File

 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document

Identifiers

Collections

Citation

Ignacio Casuso, Felix Rico, Simon Scheuring. High-speed atomic force microscopy: Structure and dynamics of single proteins This review comes from a themed issue on Analytical Techniques Edited. Current Opinion in Chemical Biology, Elsevier, 2011, 15 ((5)), pp.704-9. ⟨10.1016/j.cbpa.2011.05.007⟩. ⟨inserm-01363295⟩

Share

Metrics

Record views

359