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Analysis of DNA interactions using single-molecule force spectroscopy
Authors:Markus Ritzefeld  Volker Walhorn  Dario Anselmetti  Norbert Sewald
Affiliation:1. Organic and Bioorganic Chemistry, Bielefeld University, Bielefeld, Germany
2. Single Molecule Biophysics, Bielefeld University, Bielefeld, Germany
Abstract:Protein–DNA interactions are involved in many biochemical pathways and determine the fate of the corresponding cell. Qualitative and quantitative investigations on these recognition and binding processes are of key importance for an improved understanding of biochemical processes and also for systems biology. This review article focusses on atomic force microscopy (AFM)-based single-molecule force spectroscopy and its application to the quantification of forces and binding mechanisms that lead to the formation of protein–DNA complexes. AFM and dynamic force spectroscopy are exciting tools that allow for quantitative analysis of biomolecular interactions. Besides an overview on the method and the most important immobilization approaches, the physical basics of the data evaluation is described. Recent applications of AFM-based force spectroscopy to investigate DNA intercalation, complexes involving DNA aptamers and peptide– and protein–DNA interactions are given.
Keywords:
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