Summary
The conformation of chymotryptic fragment C2 of bacteriorhodopsin (residues 1–71) was studied by 2D1H NMR. The fragment was solubilized in a mixture of chloroform/methanol (1∶1), 0.1 M LiClO4. Most of the resonances in1H NMR spectra of fragment C2 were assigned using phase-sensitive DQF-COSY, TOCSY, and NOESY techniques. To simplify the assignment procedure for overlapping regions of NMR spectra, an analog of fragment C2 with leucines deuterated in β-positions was used. Deuterium exchange rates for amide protons were measured in a series of TOCSY spectra. Two right-handed α-helical regions Pro8-Lys30 and Lys41-Leu62 were identified on the basis of NOE connectivities and deuterium exchange rates. The N-terminal part of the fragment (Ala.2-Gly6) adopts the helical conformation stabilized by 3 hydrogen bonds.
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Sobol, A.G., Arseniev, A.S., Abdulaeva, G.V. et al. Sequence-specific resonance assignment and secondary structure of (1–71) bacterioopsin. J Biomol NMR 2, 161–171 (1992). https://doi.org/10.1007/BF01875527
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DOI: https://doi.org/10.1007/BF01875527