【摘要】 通过分析在 5 0 %D3 TFE +5 0 %H2 O溶液中采集的WET TOCSY、WET NOESY等二维核磁共振波谱 ,确定了mHCN1通道孔隙多肽氨基酸残基的自旋系统 ;通过解析NOESY谱中的NOE相关点 ,完成了对其序列以及主链和侧链质子的全部归属。利用NOE信息进行了结构计算 ,得到其三维结构。三维结构显示mHCN1通道孔隙多肽中存在一段α螺旋。其核磁共振研究结果为更深入研究选择性离子通道的机制提供了良好的基础。更多还原

【Abstract】 Spin systems for amino acid residues in mHCN1 pore region peptide have been identified through analysis of 2D NMR spectra. The sequence-specific assignment of spin systems was obtained by NOEs correlation in WET-NOESY spectra, and the complete assignment of proton resonances for backbone and side chain has been achieved. CNS software was used to calculate the structure of mHCN1 19 aa peptide. The results show that an α- helix from residue 10 to residue 13 is formed within the pore region. The results of NMR study on mHCN1 pore peptide provide the basis for further understanding the mechanism of ion selectivity of channels.更多还原