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首页> 外文会议>Advances in biomedical research >Structure Elucidation of Biopolymers from Constrained QM/MM Calculations- from NMR Chemical Shifts to Structure and Dynamics
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Structure Elucidation of Biopolymers from Constrained QM/MM Calculations- from NMR Chemical Shifts to Structure and Dynamics

机译：从受约束的QM / MM计算中阐明生物聚合物的结构-从NMR化学位移到结构和动力学

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New computational methods are presented that use NMR data as target functions for structure elucidations. It can be shown that chemical shifts can be used for the 3D structure refinement of proteins and other biopolymers. Prerequisites are a force field, an effective method for computing structure dependent atomic charges, and a very fast method for the computation of chemical shifts (bond polarization theory - BPT). Using the COSMOS-NMR hybrid force field with semi-empirical atomic charges and chemical shifts, the calculations can be performed in every step of an MD simulation or geometry optimization.rnIn the case of liquid state NMR structure investigations of proteins, ～（13）C and ~(15)N chemical shift constraints can be added to obtain accurate structure data for the main chain and side chain carbons. This method was first applied to a zinc complex of a synthetic pseudo-peptide and to membrane active peptides. In the case of proteins chemical shifts can be used to find families of structures that represent best the conformer distribution in solution.rnChemical shifts constraints are beneficial especially in solid state NMR structure investigations. For the Ras-peptide (a 7 amino acid C-terminus of the human GTPase Ras) it is demonstrated how NMR structures can be obtained using chemical shift constraints. This peptide adopts a well defined conformation if it is anchored to the membrane. Ras is probably an example of a peptide that folds on target when binding.
机译：提出了使用NMR数据作为结构阐明目标函数的新计算方法。可以证明，化学位移可以用于蛋白质和其他生物聚合物的3D结构改进。先决条件是力场，计算与结构相关的原子电荷的有效方法以及快速计算化学位移的方法（键极化理论-BPT）。利用具有半经验原子电荷和化学位移的COSMOS-NMR杂化力场，可以在MD模拟或几何优化的每个步骤中进行计算。rn在蛋白质的液态NMR结构研究中，〜（13）可以添加C和〜（15）N化学位移约束，以获得主链和侧链碳的准确结构数据。该方法首先应用于合成假肽的锌络合物和膜活性肽。在蛋白质的情况下，化学位移可用于找到最能代表溶液中构象异构体分布的结构族。化学位移约束特别有利于固态NMR结构研究。对于Ras肽（人GTPase Ras的7个氨基酸的C端），已证明如何使用化学位移限制条件获得NMR结构。如果该肽锚定在膜上，则它具有良好定义的构象。 Ras可能是结合时在靶标上折叠的肽的一个例子。

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