Bernier J L, Hénichart J P, Helbecque N
Eur J Biochem. 1984 Jul 16;142(2):371-7. doi: 10.1111/j.1432-1033.1984.tb08297.x.
The conformational and spatial configuration of the biologically active undecapeptide physalaemin was studied using 350-MHz1H NMR. The NMR analyses suggested the existence of a strong hydrogen bond between the amide proton of the Phe7 and a carbonyl group in the N-terminal moiety, most likely the Pro4 one. Other bondings were postulated, involving the side-chain amine of Lys6 and the side-chain amide of Asn5 and respectively the side-chain carboxyl of Asp3 and the terminal amide carbonyl of Met-NH2. Thus unlike its shorter peptidic fragments, physalaemin exhibited a stable molecular structure in solution, giving some insight into the conformation required for interaction at the biological receptor of tachykinins.
使用350兆赫的1H核磁共振研究了生物活性十一肽physalaemin的构象和空间构型。核磁共振分析表明，苯丙氨酸7的酰胺质子与N端部分的一个羰基之间存在强氢键，最有可能是脯氨酸4的羰基。推测还存在其他键合，涉及赖氨酸6的侧链胺和天冬酰胺5的侧链酰胺，以及分别为天冬氨酸3的侧链羧基和甲硫氨酸-NH2的末端酰胺羰基。因此，与较短的肽片段不同，physalaemin在溶液中表现出稳定的分子结构，这为速激肽在生物受体上相互作用所需的构象提供了一些见解。
