Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR

Nicole Pfleger1, Mark Lorch, Andreas C Woerner

  • 1Institute for Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J. W. Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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