Bacteriorhodopsin

Current Opinion in Structural Biology

Volumn 11, Issue 4, 2001, Pages 415-419

  Lanyi, Janos K ^a   Luecke, Hartmut ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE AMMONIA LYASE; BACTERIORHODOPSIN; GLUTATHIONE; LYSINE; SCHIFF BASE; TYROSINE;

HYDROGEN BOND; INTERCALATION COMPLEX; ION TRANSPORT; ISOMERISM; NONHUMAN; PHOTOCHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTON TRANSPORT; REVIEW; X RAY DIFFRACTION;

BACTERIA (MICROORGANISMS);

EID: 0035425498     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00226-8     Document Type: Review

References (34)

1. Three-dimensional model of purple membrane obtained by electron microscopy
2. Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
3. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
4. Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
5. Structure of bacteriorhodopsin at 1.55 angstrom resolution
6. Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 angstrom resolution
7. Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
8. Surface of bacteriorhodopsin revealed by high-resolution electron crystallography
9. The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution
10. High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle
11. Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
12. Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
13. Coupling photoisomerization of the retinal in bacteriorhodopsin to directional transport
14. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
15. Electron-crystallographic refinement of the structure of bacteriorhodopsin
16. Titration of aspartate-85 in bacteriorhodopsin: What it says about chromophore isomerization and proton release
17. a's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin
18. Assessing the functionality of a membrane protein in a three-dimensional crystal
19. Molecular dynamics study of bacteriorhodopsin and the purple membrane
20. Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution
21. Atomic resolution structures of bacteriorhodopsin photocycle intermediates: The role of discrete water molecules in the function of this light-driven ion pump
22. Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures
23. Tight Asp-85-Thr-89 association during the pump switch of bacteriorhodopsin
24. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
25. NMR probes of vectoriality in the proton-motive photocycle of bacteriorhodopsin: Evidence for an 'electrostatic steering' mechanism
26. Local-access model for proton transfer in bacteriorhodopsin
27. Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: The local-access model
28. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
29. Transient channel opening in bacteriorhodopsin: An EPR study
30. Time-resolved X-ray diffraction reveals multiple conformations in the M-N transition of the bacteriorhodopsin photocycle
31. Light-induced rotation of a transmembrane alpha-helix in bacteriorhodopsin
32. Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
33. Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle
34. Electron diffraction studies of light-induced conformational changes in the Leu-93(Ala bacteriorhodopsin mutant