Science. 1983 Sep 9;221(4615):1064-7. doi: 10.1126/science.221.4615.1064.
Thallium ion-induced carbonyl carbon chemical shifts were compared for all of the L-residue-peptide carbonyl carbons of the gramicidin A transmembrane channel. Molecular structures were deduced by using the argument that helically equivalent and equally proximal carbonyls would exhibit essentially equivalent ion-induced chemical shifts. The transmembrane channel was found to be a head-to-head dimer with the structure of a left-handed, single-stranded beta-helix.
本文比较了杆菌肽 A 跨膜通道中所有 L-残基肽羰基碳的铊离子诱导羰基碳化学位移。通过使用这样的论点推断出分子结构,即螺旋等价且同等接近的羰基将表现出基本等同的离子诱导化学位移。研究发现,跨膜通道是一个头对头的二聚体,结构为左手单链β-螺旋。