U.S.-China Cooperative Research (Molecular Biology): ScaledProtein Folding

中美合作研究（分子生物学）：规模化蛋白质折叠

• 批准号: 9107818
• 负责人: Gordon Crippen
• 金额: $ 2.71万
• 依托单位: Regents of the University of Michigan - Ann Arbor
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 1991
• 资助国家: 美国
• 起止时间: 1991-07-15 至 1993-06-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9107818&HistoricalAwards=false
• 关键词: U.S.; China; Cooperative; Research; Molecular

This proposal addresses one of the most pressing questions in molecular biology today - how to predict the folding of globular proteins from their amino acid sequence. In collaboration with Y.H. Wang of Jilin University in China, Dr. Crippen will verify, analyze and extend preliminary observations that native protein conformations can be described very compactly in terms of Fourier and other such transforms, and that these transforms correlate strongly with the protein's amino acid sequence. The subsequent goal is to develop an algorithm for searching for low energy conformations of a protein using Fourier coefficients as the primary variables. Whether the search method amounts to molecular dynamics, some kind of local or global energy minimization, or Monte Carlo procedure, the method would first manipulate the large scale features of conformation and then later adjust the small scale details. The relation between this procedure and theories of protein folding mechanisms would be explored. This project brings together two scientists, one from China, and one from the US, who share a common interest and a novel approach to an important problem in molecular biology.

这一建议解决了当今分子生物学中最紧迫的问题之一-如何从它们的氨基酸序列预测球状蛋白的折叠。克里彭博士将与中国吉林大学的王y.h.合作，验证、分析和扩展初步观察，即天然蛋白质的构象可以用傅里叶变换和其他类似的变换来非常简洁地描述，这些变换与蛋白质的氨基酸序列密切相关。接下来的目标是开发一种算法，以傅里叶系数作为主要变量来搜索蛋白质的低能构象。无论搜索方法是分子动力学，某种局部或全局能量最小化，还是蒙特卡罗程序，该方法都会先处理大尺度的构象特征，然后再调整小尺度的细节。这一过程与蛋白质折叠机制理论之间的关系将被探讨。这个项目汇集了两位科学家，一位来自中国，一位来自美国，他们对分子生物学中的一个重要问题有着共同的兴趣和新颖的方法。