Structural dynamics of single molecules studied with high-speed atomic force microscopy

Abstract

Introduction: 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.

Areas covered: 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.

Expert opinion: 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.

Keywords:

• atomic force microscopy
• DNA–protein interaction
• protein–protein interaction
• scanning probe microscopy

Declaration of interest

The author has no other relevant affiliations or financial involvement with any organisation or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.

Notes

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