Solution structure of phalloidin obtained by NMR spectroscopy in [D6]DMSO and molecular dynamics calculation in vacuo and in water
Solution structure of phalloidin obtained by NMR spectroscopy in [D6]DMSO and molecular dynamics calculation in vacuo and in water
复制标题
通过 [D6]DMSO 中的 NMR 光谱和真空和水中的分子动力学计算获得鬼笔环肽的溶液结构
DOI：
10.1002/jlac.199119910132
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发表时间：
1991
影响因子：
2.8
通讯作者：
T. Wein
中科院分区：
文献类型：
--
作者：
H. Kessler;T. Wein
本文用同向和异向NMR技术对毒伞环肽（1）[环状（L-丙氨酰-D-苏氨酰-L-半胱氨酰-顺式-4-羟基-L-脯氨酰-L-丙氨酰-L-巯基-L-丙氨酰-4，5-二羟基-L-亮氨酰）环状（36）硫化物]的全部质子和大部分碳共振进行了归属。来自双标架NOE实验的分子内质子-质子距离已被用作使用GROMOS的能量最小化和分子动力学计算的约束。已使用溶剂暴露的NH质子的电荷减少来最小化真空计算中的伪影。该结构已被证明是不稳定的，在真空中没有约束。因此，提出了一种程序，其中首先在真空中进行限制MD，并通过在水中进行限制或不受限制的MD进行精制。
Homo- and heteronuclear NMR techniques have been used to assign all proton and most of the carbon resonances of phalloidin (1) [cyclic(L-alanyl-D-threonyl-L-cysteinyl-cis-4-hydroxy-L-prolyl-L-alanyl-L-mercapto-L-tryptophyl-4,5-dihydroxy-L-leucyl) cyclic (36) sulfide], a toxic bicyclic heptapeptide of the poisonous mushroom Amanita phalloides. Intramolecular proton–proton distances derived from rotating-frame NOE experiments have been used as constraints in energy minimization and molecular dynamics calculations using GROMOS. Charge reduction of solvent-exposed NH protons has been used to minimize artifacts in the in vacuo calculation. The structure has been proven to be unstable without constraints in vacuo. Hence, a procedure is proposed in which first restrained MD in vacuo is performed and refinement is carried out by restrained or unrestrained MD in water.