MOLECULAR DYNAMIC SIMULATION OF THE INTERACTION OF THE ADAPTER WITH THE GENETIC

适配器与遗传相互作用的分子动力学模拟

• 批准号: 7956083
• 负责人: MARIA G KURNIKOVA
• 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/7956083
• 关键词: Biological; Biomedical Research; Characteristics; Computer Retrieval of Information on Scientific Projects Database; DNA Sequence Rearrangement; Family Study; Funding; Genetic; Glutamate Receptor; Grant; High Performance Computing; Hydrogen Bonding; Institution; Ion Channel Protein; Ions; Ligand Binding; Methodology; Muscle Rigidity; Post-Translational Protein Processing; Proteins; Research; Research Personnel; Resources; Shapes; Source; Structure; System; United States National Institutes of Health; flexibility; molecular dynamics; novel; protein 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. Using Molecular Dynamics (MD) simulations, computational protein modifications, and a novel theoretical methodology that determines structural rigidity/flexibility, we will concentrate on studying the family of ionotropic glutamate receptors (iGluR) due to their medicinal and biological importance. Also, we will continue to investigate the ion channel proteins with known and unknown tertiary structure. We will correlate flexibility of the protein structure with its functional characteristics, such as ion permeation and selectivity in open channels, and conformational rearrangements in gating. We are planning to analyze stability, i.e. rates and dynamics of formation and breakage of hydrogen bonds and hydrophobic contacts in protein systems that differ by size, flexibility, and a shape of ligand-binding cavities.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 使用分子动力学（MD）模拟，计算蛋白修饰以及确定结构刚度/柔韧性的新型理论方法，我们将由于其药物和生物学重要性而集中于研究离子型谷氨酸受体（IGLUR）家族。此外，我们将继续研究具有已知和未知三级结构的离子通道蛋白。我们将将蛋白质结构的柔韧性与其功能特征相关联，例如在开放通道中的离子渗透和选择性，以及门控的构象重排。我们计划分析稳定性，即形成的速率和动力学和氢键的断裂以及蛋白质系统中的疏水接触，这些蛋白质系统因大小，柔韧性和配体结合腔的形状而有所不同。