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: 7601319
• 负责人: William M. Southerland
• 金额: $ 0.03万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-08-01 至 2008-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7601319
• 关键词: Address; Amino Acid Sequence; Biological; Classification; Computer Retrieval of Information on Scientific Projects Database; DHFR gene; Dihydrofolate Reductase; Elements; Escherichia coli; Funding; Grant; Indium; Institution; Life; Object Attachment; 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.

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。 UW Pico(Tm)4.0文件：mcb030036p.abs 关键词： 分子动力学 摘要： 蛋白质在所有生物中都扮演着重要的生物角色。 了解蛋白质折叠是解决问题的关键因素 生物分子中的结构-功能相关性。能够 预测一个给定的蛋白质序列如何折叠成三维的 结构有望对蛋白质结构产生重大影响 预测和蛋白质设计。虽然主干在 蛋白质折叠，并不是每个肽键都是蛋白质折叠所必需的。 有必要进行系统的分析，以确定对 蛋白质可以折叠。卵裂在各部位的效果分析 沿着该结构上的序列将揭示该物种的分布 初级结构内的折叠元件。我们正在进行 大肠埃希菌天然DHFR的分子动力学模拟 和它的几个在标准温度下的圆形置换变体 对折叠元素的归属及其亲缘关系的研究 稳定性。