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Biochemists trap a chaperone machine in action

by last modified 12-10-12 06:54 AM
Biochemists trap a chaperone machine in action

The Hsp70 mechanism of action illustrating how the chaperone cycles between tight and loose binding states and so binds and releases its protein client. Credit: UMass Amherst

Molecular chaperones have emerged as exciting new potential drug targets, because scientists want to learn how to stop cancer cells, for example, from using chaperones to enable their uncontrolled growth. Now a team of biochemists at the University of Massachusetts Amherst led by Lila Gierasch have deciphered key steps in the mechanism of the Hsp70 molecular machine by "trapping" this chaperone in action, providing a dynamic snapshot of its mechanism.  More...

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