AB INITIO MODELING BASED ON CRYOEM MAP

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。 结构生物学的目标是通过实验确定或建模来系统地确定所有蛋白质的结构。近年来，三维低温电子显微镜在确定大分子组装到中分辨率(6-10？)的结构方面发挥了越来越重要的作用。虽然这些结构提供了组件及其组件在明确定义的功能状态下的快照，但分辨率限制了构建准确结构模型的能力。相比之下，基于序列的建模技术能够为分离的蛋白质或结构域产生相对健壮的结构模型。我们正在开发一种新的计算算法，使用CryoEM图作为评分函数，评估从从头开始建模产生的数千个模型。

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. Efforts in structural biology have targeted the systematic determination of all protein structures through experimental determination or modeling. In recent years, three-dimensional cryoEM has assumed an increasingly important role in determining the structures of large macromolecular assemblies to intermediate resolutions (6-10¿). While these structures provide a snapshot of the assembly and its components in well-defined functional states, the resolution limits the ability to build accurate structural models. In contrast, sequence-based modeling techniques are capable of producing relatively robust structural models for isolated proteins or domains. We are developing a new computational algorithm to use the cryoEM map as a scoring function to assess thousands of models generated from ab initio modeling.