Search results for: GROES

• A mobile loop order–disorder transition modulates the speed of chaperonin cycling

  Publication

  • F. Shewmaker
  • M. J. Kerner
  • M. Hayer-Hartl
  • G. Klein-Raina
  • C. Georgopoulos
  • S. J. Landry

  - PROTEIN SCIENCE - Year 2004

  Molecular machines order and disorder polypeptides as they form and dissolve large intermolecular interfaces, but the biological significance of coupled ordering and binding has been established in few, if any, macromolecular systems. The ordering and binding of GroES co-chaperonin mobile loops accompany an ATP-dependent conformational change in the GroEL chaperonin that promotes client protein folding. Following ATP hydrolysis,...

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• 18th European Symposium on Radiopharmacy and Radiopharmaceuticals

  Publication

  • V. Radchenko
  • J. Engle
  • C. Roy
  • J. Griswold
  • M. Nortier
  • E. Birnbaum
  • M. Brugh
  • S. Mirzadeh
  • K. John
  • M. Fassbender... and 487 others

  - EJNMMI Radiopharmacy and Chemistry - Year 2016

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