Summary
The conformation of the synthetic 32-residue polypeptide, an analog of the membrane spanning segment B (residues 34-65) ofHalobacterium halobium bacteriobpsin, incorporated into perdeuterated sodium dodecyl sulfate micelles in the presence of trifluoroethanol was investigated by1H NMR spectroscopy. The spectrum resonances were assigned by means of phase-sensitive DQF-COSY, TOCSY and NOESY techniques. Interproton nuclear Overhauser effects and deuterium exchange rates of individual NH groups were derived from two-dimensional NMR spectra. Analysis of the obtained data showed that segment B has a right-handed a-helical stretch from Lys41 to Leu62 with a kink at Pros50. Theα-helix in the C-terminal part is terminated at Gly63, which adopts a conformation typical of amino acid residues in a left-handed helix. The N-terminal part (residues 34–40) has no ordered conformation. NMR data are provided for comparison of the segment B conformation in the isotropic system of an organic solvent, in SDS micelles and in the purple membrane bacterioopsin. Factors affecting the conformation of membrane spanning segment B in various milieus are discussed.
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Dedicated to the memory of Professor V.F. Bystrov
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Pervushin, K.V., Arseniev, A.S., Kozhich, A.T. et al. Two-dimensional NMR study of the conformation of (34–65)bacterioopsin polypeptide in SDS micelles. J Biomol NMR 1, 313–322 (1991). https://doi.org/10.1007/BF02192857
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DOI: https://doi.org/10.1007/BF02192857