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...
المؤلفون الرئيسيون: | Ulrich, A, Heyn, M, Watts, A |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1992
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مواد مشابهة
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Distorted structure of the retinal chromophore in bacteriorhodopsin resolved by 2H-NMR.
حسب: Ulrich, A, وآخرون
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Re-orientation of retinal in the M-photointermediate of bacteriorhodopsin.
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منشور في: (1995) -
Deuterium-MAS NMR spectroscopy on oriented membrane proteins: Applications to photointermediates of bacteriorhodopsin
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Protein-lipid interactions is bacteriorhodopsin studied by solid state NMR
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منشور في: (2000) -
Structural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy.
حسب: Kamihira, M, وآخرون
منشور في: (2005)