Affiliation:
1. The authors are in the Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.
Abstract
Chemical dynamics in proteins are discussed, with bacteriorhodopsin serving as a model system. Ultrafast time-resolved methods used to probe the chemical dynamics of retinal photoisomerization in bacteriorhodopsin are discussed, along with future prospects for ultrafast time-resolved crystallography. The photoisomerization of retinal in bacteriorhodopsin is far more selective and efficient than in solution, the origins of which are discussed in the context of a three-state model for the photoisomerization reaction coordinate. The chemical dynamics are complex, with the excited-state relaxation exhibiting a multiexponential decay with well-defined rate constants. Possible origins for the two major components are also discussed.
Publisher
American Association for the Advancement of Science (AAAS)
Reference79 articles.
1. S̆rajer V., et al., Science 274, 1726 (1996);
2. Perman B., et al., ibid. 279, 1946 (1998).
3. A joint collaboration among P. A. Anfinrud K. Moffat G. N. Phillips Jr. and M. Wulff was established to investigate ligand docking sites and pathways in myoglobin with 100-ps time resolution.
4. Brilliance refers to the x-ray flux that can be delivered to a small sample that is distant from the source. All other things equal sources with smaller dimensions smaller divergence or larger flux have greater brilliance.
5. Femtosecond X-ray Pulses at 0.4 Å Generated by 90° Thomson Scattering: A Tool for Probing the Structural Dynamics of Materials
Cited by
265 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献