SIMPLIFIED MODELS FOR PROTEIN FOLDING KINETICS & THERMODYNAMICS & MECHANISM

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。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，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取得了进展。已经开发了一种程序，将全原子蛋白质结构提炼成一组电位，然后将其应用于简单的蛋白质表示。迄今为止，这些简化的蛋白质模型已经对超过20种蛋白质进行了详细的表征，并被证明特别有助于确定在共享拓扑结构的蛋白质折叠中实验观察到的定性差异的起源。这些模型也被证明比仅依赖于蛋白质拓扑结构的相关类ising模型具有相当大的优势。生成这些势的算法已经作为一个基于网络的工具（http://mmtsb.scripps.edu/webservices/gomodel.html）实现，为用户提供了一组研究他们感兴趣的蛋白质的势。

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.