Protein analysis by time-resolved measurements with an electro-switchable DNA chip

Andreas Langer, Paul A. Hampel, Wolfgang Kaiser, Jelena Knezevic, Thomas Welte, Valentina Villa, Makiko Maruyama, Matej Svejda, Simone Jähner, Frank Fischer, Ralf Strasser and Ulrich Rant ()
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Andreas Langer: Technische Universität München
Paul A. Hampel: Technische Universität München
Wolfgang Kaiser: Technische Universität München
Jelena Knezevic: Technische Universität München
Thomas Welte: Technische Universität München
Valentina Villa: Technische Universität München
Makiko Maruyama: Technische Universität München
Matej Svejda: Technische Universität München
Simone Jähner: Technische Universität München
Frank Fischer: Technische Universität München
Ralf Strasser: Technische Universität München
Ulrich Rant: Technische Universität München

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: Abstract Measurements in stationary or mobile phases are fundamental principles in protein analysis. Although the immobilization of molecules on solid supports allows for the parallel analysis of interactions, properties like size or shape are usually inferred from the molecular mobility under the influence of external forces. However, as these principles are mutually exclusive, a comprehensive characterization of proteins usually involves a multi-step workflow. Here we show how these measurement modalities can be reconciled by tethering proteins to a surface via dynamically actuated nanolevers. Short DNA strands, which are switched by alternating electric fields, are employed as capture probes to bind target proteins. By swaying the proteins over nanometre amplitudes and comparing their motional dynamics to a theoretical model, the protein diameter can be quantified with Angström accuracy. Alterations in the tertiary protein structure (folding) and conformational changes are readily detected, and even post-translational modifications are revealed by time-resolved molecular dynamics measurements.

Date: 2013
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DOI: 10.1038/ncomms3099

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