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.