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Volume 12 Issue 8, August 2016

The Hsp90 chaperone resembles a molecular clamp that opens and closes in response to ATP binding and hydrolysis. The cover features the use of high-resolution fluorescence probes consisting of a dye molecule (orange/red) and the amino acid tryptophan (blue/green) to detect changes in Hsp90 conformational motion through photo-induced electron transfer (PET)-mediated quenching of fluorescence by tryptophan residues in the protein. The background depicts the dynamic Hsp90 conformations observed by PET fluorescence, showing proteins in the open (gold molecules) and closed (blue molecules) conformations. Cover design by Erin Dewalt, based on an image created by Laurence Pearl. Article, p628; News and Views, p576

Volume 12 Issue 8

Research Highlights

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News & Views

  • Hsp90 is an energy-consuming molecular chaperone that activates oncogenic proteins in a complicated multi-step reaction. Photoinduced electron transfer (PET) quenching experiments with a fluorescent reporter have now identified molecular transitions at multiple timescales in the chaperone cycle of Hsp90.

    • Hagen Hofmann
    News & Views
  • Glucose metabolism has long been thought to operate with exquisite specificity and near-optimal efficiency. New findings show, however, that two glycolytic enzymes produce minor products that inhibit other enzymes involved in central carbon metabolism unless they are further metabolized by a novel enzyme.

    • Maria V Liberti
    • Jason W Locasale
    News & Views
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