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的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 UW皮科（tm）4.0 File：Zhongnanjiang.jpg 保留字： 分子动力学 摘要： 蛋白质在所有生物体中起着重要的生物学作用。 理解蛋白质折叠是解决蛋白质折叠问题的关键因素。 生物分子结构-功能相关性。能够 预测一个给定的蛋白质序列如何折叠成一个三维的 预期结构对蛋白质结构具有显著影响 预测和蛋白质设计。虽然主干在 蛋白质折叠，不是每一个蛋白质折叠所需的肽键。 有必要进行系统的分析，以确定 蛋白质折叠分析所有位置处的裂解效应 沿着构造上的层序， 在主结构内折叠元件。我们正在进行 大肠杆菌天然DHFR的分子动力学模拟 在标准温度下， 为了分配折叠元素并研究它们的相对位置， 稳定性