A convenient method for determining cyclic peptide conformation from 1D 1H-NMR information.
A convenient method for determining cyclic peptide conformation from 1D 1H-NMR information.
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一种根据 1D 1H-NMR 信息确定环肽构象的便捷方法。
DOI：
10.1111/j.1399-3011.1996.tb00823.x
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Bartlett,PA
中科院分区：
文献类型：
--
作者：
Sefler,AM;Lauri,G;Bartlett,PA
将ID 1H NMR信息与分子模拟相结合，建立了一种快速、简便的确定环肽骨架构象的方法。根据3 JHN，Hx耦合常数计算的Φ，角度扭转约束用于确定多阱势能罚函数的位置，该罚函数施加在结构细化中使用的力场上（Amber* 和GB/SA溶剂化模型）。蒙特卡罗搜索和最小化产生了一系列结构，这些结构通过骨架相似性进行聚类，然后根据酰胺质子的化学位移温度依赖性确定的氢键约束进行过滤。这种方法被应用到五个环肽，其结构已被确定以前使用更广泛的2D NMR技术，和扭转的重要性。评估了氢键和溶剂化限制。对于采用主要构象的四种肽，该方法紧密地再现了所报道的结构;第五种结构缺乏收敛性反映了该大环采用的多个骨架构象。© Munksgaard 1996.
A rapid and convenient method for determining the backbone conformation of cyclic peptides results from the combination of ID1H NMR information and molecular modeling. Φ, Angle torsional constraints calculated from3JHN,Hxcoupling constants are used to determine the position of multiple‐welled potential energy penalty functions that are imposed on the force field used in the structure refinement (Amber* with GB/SA solvation model). Monte Carlo searches and minimizations lead to a collection of structures that are clustered by backbone similarity and then filtered according to hydrogen‐bonding constraints determined by the chemical shift temperature dependencies of the amide protons. This approach was applied to five cyclic peptides whose structures had been determined previously using more extensive 2D NMR techniques, and the importance of the torsional. H‐bonding, and solvation restraints were assessed. For the four peptides that adopt a predominant conformation, this method reproduced the reported structures closely; lack of convergence for the fifth structure reflected the multiple backbone conformations that this macrocycle adopts. © Munksgaard 1996.