SIMPLIFIED MODELS FOR PROTEIN FOLDING KINETICS & THERMODYNAMICS & MECHANISM

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。 该项目旨在开发用于蛋白质折叠研究的快速低分辨率模型，以探索折叠动力学和热力学。在使用简单模型解决与蛋白质折叠动力学和机制有关的问题方面已经取得了进展。已经开发出一种将全原子蛋白质结构提取成一组势的程序，然后将其应用于简单的蛋白质表示。到目前为止，这些简化的蛋白质模型已经对20多种蛋白质进行了详细的表征，并被证明特别有助于确定实验观察到的共有拓扑蛋白质折叠质量差异的来源。这些模型也被证明比只依赖于蛋白质拓扑的相关类伊辛模型具有相当大的优势。用于产生这种潜力的算法已经被实现为基于网络的工具(http://mmtsb.scripps.edu/webservices/gomodel.html)，，为用户提供一组用于研究他们感兴趣的蛋白质的潜力。

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. This project is directed toward the development of rapid low-resolution models for protein folding studies exploring both folding kinetics and thermodynamics. Progress has been made in addressing questions relating to protein folding kinetics and mechanisms using simple models. A procedure has been developed to distill an all-atom protein structure into a set of potentials, which then are applied to a simple protein representation. These simplified protein models have been characterized in detail for over 20 proteins to date, and have proved particularly helpful in identifying the origins of experimentally observed qualitative differences in the folding of proteins of shared topology. These models have also been shown to offer considerable advantage over a related class of Ising-like models that depend only on the protein topology. The algorithm for generating such potentials has been implemented as a web-based tool (http://mmtsb.scripps.edu/webservices/gomodel.html), offering users a set of potentials for studying their protein of interest.