University of Minnesota
School of Physics & Astronomy
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Elias Puchner

Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules
Puchner EM and Gaub HE , Angewandte Chemie 49, 1147-50 (2010)

Download from http://onlinelibrary.wiley.com/doi/10.1002/anie.200907116/abstract

Abstract

The molecular-force sensor titin kinase (TK) is embedded in the M-band structure of the sarcomere at an ideal position to sense force imbalances. H. E. Gaub and E. M. Puchner demonstrate in their Communication on page 1147 ff. a new AFM-based single-molecule pump-and-probe protocol to mechanically prepare different conformations of TK and to read out their function. The results show that the binding pocket for the co-substrate ATP is shielded by two sequential barriers in the force-induced activation pathway.