Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR.
The orientation and conformation of retinal within bacteriorhodopsin of the purple membrane of Halobacterium halobium was established by solid-state deuterium NMR spectroscopy, through the determination of individual chemical bond vectors. The chromophore ([2,4,4,16,16,17,17,17,18,18-2H11]retinal) w...
Hlavní autoři: | Ulrich, A, Heyn, M, Watts, A |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
1992
|
Podobné jednotky
-
Distorted structure of the retinal chromophore in bacteriorhodopsin resolved by 2H-NMR.
Autor: Ulrich, A, a další
Vydáno: (1994) -
Re-orientation of retinal in the M-photointermediate of bacteriorhodopsin.
Autor: Ulrich, A, a další
Vydáno: (1995) -
Deuterium-MAS NMR spectroscopy on oriented membrane proteins: Applications to photointermediates of bacteriorhodopsin
Autor: Glaubitz, C, a další
Vydáno: (1999) -
Protein-lipid interactions is bacteriorhodopsin studied by solid state NMR
Autor: Mason, J, a další
Vydáno: (2000) -
Structural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy.
Autor: Kamihira, M, a další
Vydáno: (2005)