Nuclear-magnetic-resonance studies on the conformation of membrane-bound α-mating factor
Nuclear-magnetic-resonance studies on the conformation of membrane-bound α-mating factor
复制标题
膜结合α交配因子构象的核磁共振研究
DOI：
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发表时间：
1986
期刊：
影响因子：
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通讯作者：
T. Miyazawa
中科院分区：
文献类型：
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作者：
K. Wakamatsu;A. Okada;M. Suzuki;T. Higashijima;Y. Masui;S. Sakakibara;T. Miyazawa
对α交配因子酵母信息素在2H2O溶液中的C-H质子共振进行了归属。结果表明，双棕榈酰甘油磷胆碱悬浮液的相变温度为35.5℃。在该磷脂小泡存在的情况下，分析了50℃下多肽质子共振的交换展宽和转移核Overhauser效应(TRNOE)。阐明了该多肽与磷脂双层的结合方式。N端的9个残基(Trp1-Gly9)与双层紧密结合，而C端的4个残基(Gln10-Tyr13)在水相中保持自由。这与先前的观察一致，即C末端的三个残基(Pro11-Tyr13)对这种信息素的活性不是必需的[Masui，Y.等人。(1977)生物化学。生物群落。[中英文摘要]Re.Commun.78,534-538]。此外，通过TRNOE分析，阐明了α交配因子的膜结合N-末端部分的构象：Trp1-Gln5残基形成紧凑的螺旋结构，而Lys7-Gly9残基形成延伸结构。活性十肽类似物Trp1-Gln10也观察到类似的TRNOE。这证实了先前的结论，即这种信息素和类似肽的生理活性与膜结合肽分子的构象有关[Higashijima，T.等人。(1983)FEBS Lett.159,229-232]。
The C-H proton resonances of α-mating factor, yeast pheromone, in 2H2O solution were assigned. The phase transition temperature of perdeuterated dipalmitoylglycerophosphocholine (suspension) was found to be 35.5°C. In the presence of vesicles of this phospholipid, the exchange broadening and transferred nuclear Overhauser effect (TRNOE) of peptide proton resonances (at 50°C) were analyzed. The mode of binding of this peptide with the phospholipid bilayer was elucidated. The N-terminal nine residues (Trp1– Gly9) are tightly bound to the bilayer, while the C-terminal four residues (Gln10– Tyr13) are left free in aqueous phase. This is consistent with the previous observation that the C-terminal three residues (Pro11– Tyr13) are not essential for the activity of this pheromone [Masui, Y. et al. (1977) Biochem. Biophys. Res. Commun. 78, 534–538]. Furthermore, from the TRNOE analyses, the conformation of the membrane-bound N-terminal part of α-mating factor was elucidated: the residues Trp1– Gln5 form a compact helical structure while the residues Lys7– Gly9 form an extended structure. A similar TRNOE was also observed for an active decapeptide analog Trp1– Gln10. This confirms the previous conclusion that the physiological activities of this pheromone and analog peptides are correlated with the conformations of membrane-bound peptide molecules [Higashijima, T. et al. (1983) FEBS Lett. 159, 229–232].