MOLECULAR DYNAMICS SIMULATION OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE AND I

大肠杆菌二氢叶酸还原酶和I的分子动力学模拟

• 批准号: 7956088
• 负责人: William M. Southerland
• 金额: $ 0.08万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-08-01 至 2010-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7956088
• 关键词: Address; Amino Acid Sequence; Biological; Biomedical Research; Classification; Computer Retrieval of Information on Scientific Projects Database; DHFR gene; Dihydrofolate Reductase; Elements; Escherichia coli; Funding; Grant; High Performance Computing; Indium; Institution; Life; Organism; Peptide Sequence Determination; Peptides; Play; Positioning Attribute; Proteins; Relative (related person); Research; Research Personnel; Resources; Role; Source; Structure; Temperature; United States National Institutes of Health; Variant; Vertebral column; abstracting; design; molecular dynamics; protein folding; protein structure prediction; three dimensional structure

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. UW PICO(tm) 4.0 File: mcb030036p.abs Keywords: molecular dynamics Abstract: Proteins play an important biological role in all living organisms. Understanding protein folding is a key element in addressing a structure-function correlation in biological molecules. Being able to predict how a given protein sequence folds into a three dimensional structure is expected to have a significant impact on protein structure prediction and protein design. While the backbone plays a key role in protein folding, not every peptide bond is required for a protein to fold. A systematic analysis is necessary to identify regions essential for a protein to fold. Analysis of the effects of cleavage at all positions along the sequence on the structure will reveal the distribution of the folding elements within the primary structure. We are carrying out molecular dynamics simulations of the native DHFR from Escherichia coli and several of its circular permuted variants at standar temperature in order to assign the folding elements and to study their relative stabilities.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 华盛顿大学 PICO(tm) 4.0 文件：mcb030036p.abs 关键词： 分子动力学 抽象的： 蛋白质在所有生物体中发挥着重要的生物学作用。 了解蛋白质折叠是解决这一问题的关键要素 生物分子的结构-功能相关性。能够 预测给定的蛋白质序列如何折叠成三维 结构预计会对蛋白质结构产生重大影响 预测和蛋白质设计。虽然骨干在其中起着关键作用 蛋白质折叠，并非每个肽键都需要蛋白质折叠。 需要进行系统分析来确定对 蛋白质折叠。分析所有位置裂解的影响 沿着结构上的顺序将揭示 主要结构内的折叠元件。我们正在执行 大肠杆菌天然 DHFR 的分子动力学模拟 及其在标准温度下的几个圆形排列变体 为了分配折叠元素并研究它们的相关性 稳定性。