Abstract
Force spectroscopy has developed into an indispensable tool for studying folding and binding of proteins on a single molecule level in real time. Design of the pulling geometry allows tuning the reaction coordinate in a very precise manner. Many recent experiments have taken advantage of this possibility and have provided detailed insight the folding pathways on the complex high dimensional energy landscape. Beyond its potential to provide control over the reaction coordinate, force is also an important physiological parameter that affects protein conformation under in vivo conditions. Single molecule force spectroscopy studies have started to unravel the response and adaptation of force bearing protein structures to mechanical loads.
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