Esposito G, Carver J A, Boyd J, Campbell I D
Biochemistry. 1987 Feb 24;26(4):1043-50. doi: 10.1021/bi00378a010.
A 1H NMR study of the peptide alamethicin, which forms voltage-gated ion channels in membranes, is described. The molecule was studied in methanol as a function of temperature and pH. A complete assignment of the spectra is given, including several stereospecific assignments. Alamethicin was found to have a structure substantially similar to the crystal although, in solution, the C-terminal dipeptide adopts a somewhat extended conformation. The overall conformation was insensitive to the ionization of the side chain of the only ionizable group, Glu-18.
本文描述了对在膜中形成电压门控离子通道的短杆菌肽A进行的¹H NMR研究。该分子在甲醇中作为温度和pH的函数进行了研究。给出了光谱的完整归属，包括几个立体特异性归属。尽管在溶液中，C端二肽采取了某种伸展构象，但发现短杆菌肽A的结构与晶体基本相似。整体构象对唯一可电离基团Glu-18侧链的电离不敏感。
