Smart O S, Goodfellow J M, Wallace B A
Department of Crystallography, Birkbeck College, University of London, England.
Biophys J. 1993 Dec;65(6):2455-60. doi: 10.1016/S0006-3495(93)81293-1.
The ion channel forming peptide gramicidin A adopts a number of distinct conformations in different environments. We have developed a new method to analyze and display the pore dimensions of ion channels. The procedure is applied to two x-ray crystal structures of gramicidin that adopt distinct antiparallel double helical dimer conformations and a nuclear magnetic resonance (NMR) structure for the beta6.3 NH2-terminal to NH2-terminal dimer. The results are discussed with reference to ion conductance properties and dependence of pore dimensions on the environment.
形成离子通道的肽短杆菌肽A在不同环境中会呈现多种不同的构象。我们开发了一种新方法来分析和展示离子通道的孔径。该方法应用于短杆菌肽的两种X射线晶体结构,这两种结构呈现出不同的反平行双螺旋二聚体构象,以及β6.3 NH2末端到NH2末端二聚体的核磁共振(NMR)结构。结合离子传导特性以及孔径对环境的依赖性对结果进行了讨论。