Arsen'ev A S, Chikin L D, Kozhich A T, Ivanov V T
Bioorg Khim. 1993 Jan;19(1):5-20.
Conformations of synthetic peptides, analogues of the membrane spanning segments C (residues 67-106), E (128-162) and G (190-233) of bacteriorhodopsin Halobacterium halobium were studied by two-dimensional 1H-NMR spectroscopy. Peptides were solubilized in the mixture chloroform-methanol (1:1), 0.1 M LiC1O4. The spectrum resonances were assigned by means of phase-sensitive DQF-COSY, TOCSY and NOESY techniques. Interproton nuclear Overhauser effects were derived from NOESY spectra. Amide protons with slow deuterium exchange rates were determined. Analysis of the obtained data showed that segments C, E and G form right-handed alpha-helices including residues 77-101, 131-159 and 198-227, respectively.
通过二维¹H-NMR光谱研究了嗜盐菌视紫红质嗜盐栖热菌跨膜片段C（残基67 - 106）、E（128 - 162）和G（190 - 233）类似物的合成肽构象。将肽溶解在氯仿 - 甲醇（1:1）、0.1 M LiC1O₄的混合物中。通过相敏DQF-COSY、TOCSY和NOESY技术对光谱共振进行了归属。质子间核Overhauser效应源自NOESY光谱。确定了氘交换速率缓慢的酰胺质子。对所得数据的分析表明，片段C、E和G分别形成了包含残基77 - 101、131 - 159和198 - 227的右手α-螺旋。
