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Thursday, 12 January, 2012

Energy saving chaperone Hsp90

Large conformational changes without ATP consummation

A special group of proteins, the so-called chaperones, helps other proteins to obtain their correct conformation. Until now scientists supposed that hydrolyzing ATP provides the energy for the large conformational changes of chaperone Hsp90. Now a research team from the Nanosystems Initiative Munich (NIM) could prove that Hsp90 utilizes thermal fluctuations as the driving force for its conformational changes. The renowned journal PNAS reports on their findings.

 

Press information TUM (english)
Presseinformation der TUM (deutsch)
Publication "Heat shock protein 90’s mechano-chemical cycle is dominated by thermal fluctuations"