Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR.

Journal article

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) was specifically deuterium-labeled on the cyclohexene ring and incorporated into the protein. A uniaxially oriented sample of purple membrane patches was prepared and measured at a series of inclina...

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Authors: Ulrich, A; Heyn, M; Watts, A

• Publication status: Published
• Journal: Biochemistry
• Volume: 31
• Issue: 42
• Pages: 10390-10399
• Publication date: 1992-10-01
• DOI: 10.1021/bi00157a029
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Deuterium; Halobacterium salinarum; Mathematics; Bacteriorhodopsins; Macromolecular Substances; Protein Conformation; Magnetic Resonance Spectroscopy; Retinaldehyde; Molecular Conformation; Molecular Structure