SIMPLIFIED MODELS FOR PROTEIN FOLDING KINETICS & THERMODYNAMICS & MECHANISM

蛋白质折叠动力学的简化模型

• 批准号: 7358848
• 负责人: CHARLES L BROOKS
• 金额: $ 1.1万
• 依托单位: SCRIPPS RESEARCH INSTITUTE, THE
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-09-01 至 2007-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7358848
• 关键词: SIMPLIFIED; MODELS; PROTEIN; FOLDING; KINETICS

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.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。该项目是针对蛋白质折叠研究探索折叠动力学和热力学的快速低分辨率模型的发展。利用简单的模型解决蛋白质折叠动力学和机制的相关问题已经取得了进展。一个程序已经开发到一组潜在的，然后被应用到一个简单的蛋白质表示提取的全原子蛋白质结构。这些简化的蛋白质模型已经详细描述了20多个蛋白质，并已证明特别有助于确定实验观察到的共享拓扑结构的蛋白质折叠的定性差异的起源。这些模型也被证明提供了相当大的优势，比相关的一类伊辛样模型，只依赖于蛋白质的拓扑结构。用于生成这种电位的算法已经被实现为基于网络的工具（http：//mmtsb.scripps.edu/webservices/gomodel.html），为用户提供一组电位以用于研究他们感兴趣的蛋白质。