NMR REFINEMENT

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目及 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 在NMR结构计算的能量函数中，静电相互作用经常被过度简化或忽略，因为如果没有适当描述溶剂的介电屏蔽，就很难可靠地评估它们。在最近的改进隐式溶剂模型，它表明，模拟退火细化在GB隐式溶剂中可能会导致显着的改善，在最终的蛋白质NMR结构的骨架二面角分布和氢键模式。然而，当存在足够数量的实验约束时（例如在NMR结构测定的最后阶段），隐式溶剂的影响相当小。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Electrostatic interactions are often oversimplified or ignored in the energy functions for NMR structure calculations, because it is difficult to evaluate them reliably without proper description of the dielectric screening by solvent. In light of recent improvements in implicit solvent models, it was showed that simulated annealing refinement in a GB implicit solvent could lead to noticeable improvement in the final protein NMR structures in terms of the backbone dihedral angle distributions and hydrogen bond patterns. However, the impact of implicit solvent is rather small when a sufficient number of experimental restraints exist (such as in the final stage of NMR structure determination).