We thank M. Gautel, his colleagues A. Alexandrovich and B. Brandmeier for the titin kinase protein constructs, and S. Stahl, A. Fornof, and H. Engelke for helpful diskussions. E.M.P. thanks the international Doktorate Program NanoBioTechnology (IDK-NTB) for support. This work was funded by the Deutsche Forschungsgemeinschaft.
Exploring the Conformation-Regulated Function of Titin Kinase by Mechanical Pump and Probe Experiments with Single Molecules†
Article first published online: 13 JAN 2010
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 49, Issue 6, pages 1147–1150, February 1, 2010
How to Cite
Puchner, Elias M. and Gaub, Hermann E. (2010), Exploring the Conformation-Regulated Function of Titin Kinase by Mechanical Pump and Probe Experiments with Single Molecules. Angew. Chem. Int. Ed., 49: 1147–1150. doi: 10.1002/anie.200905956
- Issue published online: 26 JAN 2010
- Article first published online: 13 JAN 2010
- Manuscript Received: 22 OCT 2009
- Deutsche Forschungsgemeinschaft
- force spectroscopy;
- scanning probe microscopy;
- single-molecule studies
Feel the force: A new AFM-based single-molecule pump-and-probe protocol has been used to investigate the function of different force-induced conformations of proteins (see picture). It was found that the autoinhibited enzyme titin kinase reaches its ability to bind ATP after the first two barriers of the complex mechanical activation pathway.