Conformation of the synthetic 32-residue polypeptide, an analog of membrane spanning segment B (residues 34-65) of the Halobacterium halobium bacteriorhodopsin in the membrane mimetic system, methanol/chloroform (1:1), was investigated by 1H-NMR spectroscopy. Previously it was shown by 19F-NMR spectroscopy that this medium retains the native conformation of membrane bound BR and its fragments. The spectrum resonance was assigned by means of the sequential signal assignment porcedure using phase-sensitive DQF-COSY, MLEV17 HOHAHA and NOESY techniques. Interproton nuclear Overhauser effects, spin-spin coupling constant of vicinal H-NCα-H protons and deuterium exchange rates of individual NH groups were derived from two-dimensional NMR spectra. The data unequivocally define the peptide conformation as the right-handed α-helix, extremely rigid in the central region from Phe 42 to Nle 60 and flexible in the N- and C-terminal parts. © 1988.
Arseniev, A. S., Maslennikov, I. V., Bystrov, V. F., Kozhich, A. T., Ivanov, V. T., & Ovchinnikov, Y. A. (1988). Two-dimensional 1H-NMR study of bacterioopsin-(34-65)-polypeptide conformation. FEBS Letters, 231(1), 81–88. https://doi.org/10.1016/0014-5793(88)80707-5