Dynamic imaging of single DNA–protein interactions using atomic force microscopy

Atomic force microscopy (AFM) imaging of static DNA–protein complexes, in air and in liquid, can be used to directly obtain quantitative and qualitative information on the structure of different complexes. For example, DNA length, the location of preferential binding sites for proteins and bending o...

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Bibliographic Details
Published in:Analytica Chimica Acta 2003-03, Vol.479 (1), p.3-15
Main Authors: Bennink, Martin L., Nikova, Dessy N., van der Werf, Kees O., Greve, Jan
Format: Article
Language:English
Subjects:
Analytical chemistry
Atomic force microscopy
Chemistry
DNA
Dynamics
Exact sciences and technology
Interactions
Protein
Spectrometric and optical methods
Structure
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Summary:Atomic force microscopy (AFM) imaging of static DNA–protein complexes, in air and in liquid, can be used to directly obtain quantitative and qualitative information on the structure of different complexes. For example, DNA length, the location of preferential binding sites for proteins and bending of DNA as a result of the complexation can all be measured. Recording consecutive AFM images of DNA and protein molecules under conditions that they are still able to move and interact, or dynamic AFM imaging, however, can reveal information on the dynamic aspects of the interactions between these molecules. Here, an overview is given of the technical challenges that need to be considered for successful dynamic AFM imaging studies of individual DNA–protein interactions. Necessary technical improvements to the AFM set-up and the development of new sample preparation methods are described in this paper.
ISSN:0003-2670
1873-4324
DOI:10.1016/S0003-2670(02)01571-4