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Chaperone Proteins in the Crash Test

Each and every protein in a living organism is tightly regulated by input signals to allow the cell to respond to its environment. How can such a signal switch a protein on or off? Using high-performance computer simulations and novel ways of analysing forces within proteins, a team of scientists of the Molecular Biomechanics Group at the Heidelberg Institute of Theoretical Studies (HITS) under leadership of Dr. Frauke Gräter analysed how the heat shock protein Hsp90, a helper protein vital to any cell in any organism, is switched by the binding of a small molecule. Within the very complex structure of this protein-molecular machine, the scientists could identify a network of forces spanning from the binding site of the small molecule to a hinge region. The computed network helps to understand the way such a helper protein works and might lead to new avenues for the design of anti-cancer agents targeted to Hsp90.

Binding of a small molecule (black) ho Hsp90 (grey)Binding of a small molecule (black) to Hsp90 (grey) gives rise to a force network that can explain how this protein is functionally regulated.
Source: HITS gGmbH, Heidelberg

Dr. Frauke Gräter
Group Leader, Molecular Biomechanics - HITS gGmbH
D-69118 Heidelberg
e-mail: Frauke.Graeter@h-its.org

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