The final stages of folding of the membrane protein bacteriorhodopsin occur by kinetically indistinguishable parallel folding paths that are mediated by pH

Journal of Molecular Biology

Volumn 299, Issue 1, 2000, Pages 233-243

  Lu, Hui ^a   Booth, Paula J ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Bacteriorhodopsin; Membrane protein folding; Parallel pathways; Retinal binding; Side chain ionisation

Indexed keywords

BACTERIORHODOPSIN; GUANINE; LYSINE; MEMBRANE PROTEIN; MUTANT PROTEIN; RETINAL;

ARTICLE; CONCENTRATION RESPONSE; COVALENT BOND; ISOMERISM; KINETICS; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS);

EID: 0034716941     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3735     Document Type: Article

References (43)

1. Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties
2. Prediction of pH-dependent properties of proteins
3. Theoretical-study of color control mechanism in retinal proteins. 2. Orientational effects of aromatic amino acid residues upon opsin shift
4. Theoretical-study of color control mechanism in retinal proteins. 1. Role of the tryptophan residue, tyrosine residue and water molecule
5. Folding α helical membrane proteins: Kinetic studies on bacteriorhodopsin
6. Membrane protein folding
7. Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy
8. Intermediates in the folding of the membrane protein bacteriorhodopsin
9. Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin
10. Evidence that bilayer bending rigidity affects membrane protein folding
11. Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Eschericia coli
12. How important is the molten globule for correct protein folding?
13. Kinetic evidence for an obligatory intermediate in the folding of the membrane protein bacteriorhodopsin
14. Changes in the protonation state of bacterio-opsin during reconstitution of bacteriorhodopsin
15. Removal of methyl groups from retinal controls the activity of bacteriorhodopsin
16. Closing in on bacteriorhodopsin: Progress in understanding the molecule
17. Evidence for an obligatory intermediate in the folding of interleukin-1β
18. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
19. Classical electrostatics in biology and chemistry
20. Physical origin of the opsin shift of bacteriorhodopsin. Comprehensive analysis based on medium effect theory of absorption spectra
21. Refolding of an integral membrane protein. Denaturation, renaturation and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
22. Two light-transducing membrane proteins: Bacteriorhodopsin and the mammalian rhodopsin
23. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
24. Regeneration of the native bacteriorhodopsin structure from two chymotryptic fragments
25. Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
26. Circular dichroism of biological membranes: Purple membrane of Halobacterium halobium
27. An external point-charge model for bacteriorhodopsin
28. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
29. Formation of electrostatic interactions on the protein-folding pathway
30. Thermodynamics of transient conformations in the folding pathway of barnase: Reorganisation of the folding intermediate at low pH
31. Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength; evidence for residual electrostatic interactions in the acid/thermally denatured state
32. The folding of hen lysozyme involves partially structured intermediates and multiple pathways
33. Slow α helical formation during folding of a membrane protein
34. Structural characterization of folding intermediates in cytocheme c by H-exchange labelling and proton NMR
35. Reconstitution of bacteriorhodopsin from the apoprotein and retinal studied by fourier-transform infrared spectroscopy
36. Studies on the retinal-protein interaction in bacteriorhodopsin
37. Specificity of the retinal binding site of bacteriorhodopsin: Chemical and stereochemical requirements for the binding of retinol and retinal
38. Bacteriorhodopsin and related pigments of halobacteria
39. Electrostatic energy and macromolecular function
40. Proton translocation by bacteriorhodopsin and heme-copper oxidases
41. Folding intermediates in cytochrome c