1 FORCE-INDUCED ACTIVATION OF TALIN 2 MECHANICS AND SELF-ASSEMBLY OF THE SYNT

1 TALIN 的力诱导激活 2 SYNT 的力学和自组装

• 批准号: 7601530
• 负责人: ROGER D KAMM
• 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/7601530
• 关键词: Behavior; Binding Sites; Cells; Cereals; Computer Retrieval of Information on Scientific Projects Database; Extracellular Matrix; Funding; Grant; Institution; Measures; Mechanics; Modeling; Peptides; Property; Proteins; Research; Research Personnel; Resources; Signal Transduction; Site; Source; Talin; United States National Institutes of Health; Vinculin; molecular dynamics; scaffold; self assembly; simulation

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. We are engaged in two projects requiring molecular dynamic simulations of proteins. First, we are examining a potential mechanism of mechanotransduction by talin, a protein found at sites where a cell anchors to the extracellular matrix. Talin could begin a signaling cascade by unfolding under an applied force to expose a binding site for the protein vinculin. Second, we are investigating the mechanical and self-assembly properties of the peptide [RARADADA]2, a cell scaffold material. We use atomistic simulations to measure parameters for course-grained models of bulk material behavior.

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。 我们正在进行两个需要蛋白质分子动力学模拟的项目。首先，我们正在研究踝蛋白（talin）机械传导的潜在机制，踝蛋白是一种在细胞锚定到细胞外基质的位点发现的蛋白质。 Talin 可以通过在外力作用下展开以暴露纽蛋白蛋白的结合位点来开始信号级联反应。其次，我们正在研究肽 [RARADADA]2（一种细胞支架材料）的机械和自组装特性。我们使用原子模拟来测量散装材料行为的粗粒度模型的参数。