Exploring the Conformation-Regulated Function of Titin Kinase by Mechanical Pump and Probe Experiments with Single Molecules

Angewandte Chemie, 2010, 49 Issue 6, 1147-50 published on 13.01.2010
Angewandte Chemie, online article
Protein function such as catalytic activity or molecular recognition is tightly coupled to the conformation and dynamics. Since protein conformations may be controlled by forces, diverse active and passive mechanisms have evolved that allow biological systems to respond to mechanical signals. However, forces act in a predetermined direction on these biomolecules and are so minute that the investigation of the underlying mechanisms is difficult to achieve in ensemble experiments and has to be performed on the level of individual molecules. Atomic force microscopy (AFM) based[1] single-molecule force spectroscopy (SMFS)[2] has evolved into a powerful tool for the investigation of such biomolecules in their natural parameter space of force and extension. In addition, it provides the necessary resolution in the submolecular nanometer and pico-Newton range to control or detect intermolecular conformational changes and their related functions[3,4] and to investigate protein folding and unfolding.

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