The Hsp Mechanism (image) University of Massachusetts at Amherst Share Print E-Mail 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 Usage Restrictions None Share Print E-Mail Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert system.