NMR REFINEMENT

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 在核磁共振结构计算的能量函数中，静电相互作用往往被过分简化或忽略，因为如果没有对溶剂介电屏蔽的适当描述，很难可靠地评估静电相互作用。鉴于最近对隐式溶剂模型的改进，结果表明，在GB隐式溶剂中进行模拟退火精化可以显著改善最终蛋白质的核磁共振结构，包括主链二面角分布和氢键模式。然而，当存在足够数量的实验限制时(例如在核磁共振结构确定的最后阶段)，隐含溶剂的影响相当小。

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).