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Contact: Janet Lathrop
jlathrop@admin.umass.edu
413-545-0444
University of Massachusetts at Amherst
Caption: The Hsp70 mechanism of action illustrating how the chaperone cycles between tight and loose binding states and so binds and releases its protein client. The new work from Zhuravleva, Clerico and Gierasch enabled the key intermediate allosterically active state to be described in molecular detail, shedding light on previously mysterious aspects of Hsp70 function.
Credit: UMass Amherst
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Related news release: Biochemists trap a chaperone machine in action
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