Conformational selection in protein binding and binding-induced folding

  • Datum: 01.03.2017
  • Uhrzeit: 09:15 - 10:15
  • Vortragende(r): Dr. Thomas Weikl
  • Max Planck Institute of Colloids and Interfaces; Potsdam
  • Ort: Max-Planck-Institut für biophysikalische Chemie (MPIBPC)
  • Raum: Large Seminar Room (Administration Building)
  • Gastgeber: Prof. Dr. Christian Griesinger
  • Kontakt: sekr@nmr.mpibpc.mpg.de
The function of proteins is affected by their conformational dynamics, i.e. by transitions between lower-energy ground-state conformations and higher-energy excited-state confirmations of the proteins. Advanced NMR and single-molecule experiments indicate that higher-energy conformations in the unbound state of proteins can be similar to ground-state conformations in the bound state, and vice versa. These experiments illustrate that the conformational change of a protein during binding may occur before a binding event ('conformational selection'), rather than being induced by this binding event ('induced fit'). However, determining the temporal order of conformational transitions and binding events and, thus, distinguishing conformational-selection and induced-fit processes typically requires additional information on the binding kinetics.
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