• Medientyp: E-Artikel
  • Titel: Time-resolved observation of protein allosteric communication
  • Beteiligte: Buchenberg, Sebastian; Sittel, Florian; Stock, Gerhard
  • Erschienen: National Academy of Sciences, 2017
  • Erschienen in: Proceedings of the National Academy of Sciences of the United States of America, 114 (2017) 33, Seite E6804-E6811
  • Sprache: Englisch
  • ISSN: 0027-8424; 1091-6490
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  • Beschreibung: Allostery represents a fundamental mechanism of biological regulation that is mediated via long-range communication between distant protein sites. Although little is known about the underlying dynamical process, recent time-resolved infrared spectroscopy experiments on a photoswitchable PDZ domain (PDZ2S) have indicated that the allosteric transition occurs on multiple timescales. Here, using extensive nonequilibrium molecular dynamics simulations, a time-dependent picture of the allosteric communication in PDZ2S is developed. The simulations reveal that allostery amounts to the propagation of structural and dynamical changes that are genuinely nonlinear and can occur in a nonlocal fashion. A dynamic network model is constructed that illustrates the hierarchy and exceeding structural heterogeneity of the process. In compelling agreement with experiment, three physically distinct phases of the time evolution are identified, describing elastic response (≲0.1 ns), inelastic reorganization (∼100 ns), and structural relaxation (≳1 μs). Issues such as the similarity to downhill folding as well as the interpretation of allosteric pathways are discussed.
  • Zugangsstatus: Freier Zugang