FOR 490:  Molekulare Mechanismen von Retinal Protein Funktionen: Eine Kombination von Theoretischen Methoden und Näherungen

• Fachliche Zuordnung: Physik ; Biologie ; Chemie
• Förderung: Förderung von 2002 bis 2008
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 5469831

Keine Zusammenfassung vorhanden

• DFG-Verfahren: Forschungsgruppen

Projekte

• Computer simulation of anion pumping by retinal proteins (Antragsteller Fischer, Ph.D., Stefan )
• Computer Simulation of Conformation-Coupled Proton Transfer in Bacteriorhodopsin (Antragsteller Suhai, Sandor )
• Computer simulation of the proton transfer pathways at the extracellular side of bacteriorhodopsin and calculation of IR spectra of the photocycle intermediates (Antragsteller Suhai, Sandor )
• DFTB QM/MM calculations of retinal protein excited states (Antragsteller Elstner, Marcus )
• Excited state dynamics in the early stages of the bR and Rh photocycle (Antragsteller Frauenheim, Thomas )
• Excited state dynamics in the early stages of the bR and Rh photocycle (Antragsteller Frauenheim, Thomas )
• Mechanisms of the Opsin Shift (Antragsteller Buß, Volker )
• Mechanisms of the Opsin Shift (Antragsteller Buß, Volker )
• Molecular Mechanisms of Retinal Protein Action: Coordination Project (Antragsteller Frauenheim, Thomas )
• Proton transfer and conformational dynamics in the M2-to-O steps of the bacteriorhodopsin photocycle (Antragsteller Smith, Jeremy Christopher )
• QM/MM calculations of retinal protein excited states: Investigating the mechanisms of color tuning (Antragsteller Elstner, Marcus )
• Regulation of the Proton Pumping Activity of Bacteriorhodopsin - The influence of Membrane Potential and Proton Gradient (Antragsteller Ullmann, Matthias )
• Structures of the first intermediates of the visual cascade (Antragsteller Entel, Peter )
• Structures of the first intermediates of the visual cascade (Antragsteller Entel, Peter )

• Sprecher: Professor Dr. Thomas Frauenheim
• stellvertr. Sprecher: Professor Dr. Jeremy Christopher Smith