Solid-state NMR spectroscopy applied to membrane proteins (original) (raw)
Abstract
cross polarisation MAS magic angle spinning MD molecular dynamics PSII photosystem II Solid-state NMR spectroscopy applied to membrane proteins de Groot 599
Loading Preview
Sorry, preview is currently unavailable. You can download the paper by clicking the button above.
References (14)
- Verdegem PJE, Helmle M, Lugtenburg J, de Groot HJM: Internuclear distance measurements up to 0.44 nm for retinals in the solid state with 1-D rotational resonance 13 C MAS NMR spectroscopy. J Am Chem Soc 1997, 119:169-174.
- Verdegem PJE, Lugtenburg J, de Groot HJM: The use of isotopes for probing ligand-protein interactions and ligand structure: the rhodopsin G-protein coupled membrane receptor paradigm. In Stable Isotopes in Pharmaceutical Research. Edited by Browne TR. Amsterdam: Elsevier Science; 1997:203-217.
- Bifone A, de Groot HJM, Buda F: Energy storage in the primary photoproduct of vision. J Phys Chem 1997, 101B:2954-2958.
- Buda F, de Groot HJM, Bifone A: Charge localization and dynamics in rhodopsin. Phys Rev Lett 1996, 77:4474-4477.
- Smith SO, Courtin J, de Groot H, Gebhard R, Lugtenburg J: 13 C magic angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin. Biochemistry 1991, 30:7409-7415.
- Buss V, Kolster K, Terstegen F, Vahrenhorst R: Absolute sense of twist of the C12-C13 bond of the retinal chromophore in rhodopsin-semiempirical and non-empirical calculations of chiroptical data. Angew Chem Int Ed Engl 1998, 37:1893-1895.
- Creemers AFL, Klaassen CHW, Bovee-Geurts PHM, Kelle R, Kragl U, •• Raap J, de Grip WJ, Lugtenburg J, de Groot HJM: Solid state 15N NMR evidence for a complex Schiff base counterion in the visual G-protein coupled receptor rhodopsin. Biochemistry 1999, 38:7195-7199.
- Expression and isotope labelling of NMR quantities (several milligrams) of the rhodopsin G-protein-coupled receptor was followed by a functional assay of the active site. Using solid-state NMR, it was established that the charged chromophore in rhodopsin is stabilised by a complex counterion. 46. de Groot HJM, Harbison GS, Herzfeld J, Griffin RG: Nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin: counterion effects on the 15 N shift anisotropy. Biochemistry 1989, 28:3346-3353.
- de Groot HJM, Smith SO, Courtin J, van den berg EMM, Winkel C, Lugtenburg J, Herzfeld J, Griffin RG: Solid state 13 C and 15 N NMR study of the low pH forms of bacteriorhodopsin. Biochemistry 1990, 29:6873-6883.
- Petkova AT, Hu JGG, Bizounok M, Simpson M, Griffin RG, Herzfeld J: •• Arginine activity in the proton-motive photocycle of bacteriorhodopsin: solid state NMR studies of the wild-type and D85N proteins. Biochemistry 1999, 38:1562-1572.
- A comprehensive spectroscopic investigation into the electronic and protonic structure of the bacteriorhodopsin active site. Anomalous effects of the arginine participation in the complex counterion active site were resolved during the pro- ton pumping cycle using a combination of labels and site-specific mutagenesis.
- Griffiths JM, Bennet AE, Engelhard M, Siebert F, Raap J, Lugtenburg J, • Herzfeld J, Griffin RG: Structural investigation of the active site in bacteriorhodopsin: geometric constraints on the roles of Asp-85 and Asp-212 in the proton-pumping mechanism from solid state NMR. Biochemistry 2000, 39:362-371.
- A high-resolution assay of structural changes in the active site during the proton pumping cycle of bacteriorhodopsin in its natural environment.
- Van Rossum B-J: Structure refinement of photosynthetic components with multidimensional MAS NMR dipolar correlation spectroscopy [PhD Thesis]. Leiden: Leiden University; 2000.