THE STRUCTURE OF MELITTIN - A H-1-NMR STUDY IN METHANOL
THE STRUCTURE OF MELITTIN - A H-1-NMR STUDY IN METHANOL
复制标题
DOI：
10.1111/j.1432-1033.1988.tb13977.x
复制
发表时间：
1988-04-05
期刊：
影响因子：
--
通讯作者：
CAMPBELL, ID
中科院分区：
文献类型：
--
作者：
BAZZO, R;TAPPIN, MJ;CAMPBELL, ID
用核磁共振氢谱研究了26个氨基酸残基的多肽蜂毒肽在甲醇溶液中的构象。利用二维核磁共振技术对蜂毒肽的1H-NMR谱进行了归属，并利用距离几何和约束分子动力学分析从核Overhauser增强数据计算了其二级结构。发现该结构主要是螺旋形的，并且类似于从衍射数据在晶体中发现的结构：残基2-11和13-26形成规则的α-螺旋由残基11-12之间的“铰链"连接。在这个铰链区的结构被证明是显着不同的晶体结构，导致两个螺旋之间的角度较小。脯氨酸残基在此和类似的跨膜肽的可能意义进行了讨论。
The conformation of the 26-residue polypeptide melittin has been studied using 1H-NMR spectroscopy in methanolic solution. The 1H-NMR spectrum of melitin has been assigned using two-dimensional NMR techniques and the secondary structure has been calculated from nuclear Overhauser enhancement data using distance geometry and restrained molecular dynamics analyses. The structure is found to be mainly helical, and similar to that found in crystals from diffraction data: residues 2-11 and 13-26 form regular .alpha.-helices jointed by a ''hinge'' between residues 11-12. The structure in this hinge region is shown to be significantly different from that in the crystal structure, leading to a smaller angle between the two helices. The possible significance of the proline residues in this and similar membrane-spanning peptides is discussed.