This paper is part of the Proceedings of the 13th International Conference on Retinal Proteins, Barcelona, Spain, 15–19 June 2008.
Light-induced Modulation of Protein Dynamics During the Photocycle of Bacteriorhodopsin†
Article first published online: 13 JAN 2009
© 2009 The Authors. Journal Compilation. The American Society of Photobiology
Photochemistry and Photobiology
Volume 85, Issue 2, pages 590–597, March/April 2009
How to Cite
Pieper, J., Buchsteiner, A., Dencher, N. A., Lechner, R. E. and Hauß, T. (2009), Light-induced Modulation of Protein Dynamics During the Photocycle of Bacteriorhodopsin. Photochemistry and Photobiology, 85: 590–597. doi: 10.1111/j.1751-1097.2008.00501.x
The Helmholtz Center Berlin has recently been renamed from Hahn-Meitner-Institut Berlin.
- Issue published online: 25 FEB 2009
- Article first published online: 13 JAN 2009
- Received 18 September 2008, accepted 1 October 2008
Knowledge about the dynamical properties of a protein is of essential importance for understanding the structure–dynamics–function relationship at the atomic level. So far, however, the correlation between internal protein dynamics and functionality has only been studied indirectly in steady-state experiments by variation of external parameters like temperature and hydration. In the present study we describe a novel type of (laser-neutron) pump-probe experiment, which combines in situ optical activation of the biological function of a membrane protein with a time-dependent monitoring of the protein dynamics using quasielastic neutron scattering. As a first successful application we present data obtained selectively in the ground state and in the M-intermediate of bacteriorhodopsin (BR). Temporary alterations in both localized reorientational protein motions and harmonic vibrational dynamics have been observed during the photocycle of BR. This observation is a direct proof for the functional significance of protein structural flexibility, which is correlated with the large-scale structural changes in the protein structure occurring during the M-intermediate. We anticipate that functionally important modulations of protein dynamics as observed here are of relevance for most other proteins exhibiting conformational transitions in the time course of functional operation.