CHARACTERIZING THE CONFORMATIONAL PREFERENCES OF P53 PEPTIDES

表征 P53 肽的构象偏好

• 批准号: 7956234
• 负责人: LILLIAN T CHONG
• 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/7956234
• 关键词: Biomedical Research; Computer Retrieval of Information on Scientific Projects Database; Development; Funding; Grant; High Performance Computing; Institution; Mind; Peptide Fragments; Peptides; Protein Binding; Protein p53; Proteins; Research; Research Personnel; Resources; Rest; Running; Services; Source; TP53 gene; Transcriptional Activation Domain; United States National Institutes of Health; Writing; computing resources; molecular dynamics; preference; 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. During the next couple of months, I will be using my Development allocation of 30,000 Service Units (SUs) on the Teragrid to carry out molecular dynamics simulations to characterize, in atomistic detail, the conformational preferences of peptide fragments of the natively unfolded transcriptional activation domain of (TAD) tumor suppressor p53. While this Development allocation is not sufficient for me to perform all the required simulations, the simulations that I will be able to run will provide useful information for estimating my remaining computing needs on the Teragrid. With this information in mind, I will be writing a proposal for obtaining sufficient computational resources to complete the rest of the project. Results from these simulations will expand our understanding of the mechanisms by which so-called natively unfolded proteins, a.k.a. intrinsically unstructured proteins, bind to other partner proteins.

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。 在接下来的几个月中，我将使用我在Teragrid上的30,000个服务单元（SUS）的开发分配来执行分子动力学模拟，以在原子质细节中表征（TAD）抑制（TAD）抑制p53的原子肽片段的肽片段的构象偏好。尽管这种开发分配不足以执行所有必需的模拟，但我将能够运行的模拟将提供有用的信息，以估计我在Teragrid上的剩余计算需求。考虑到这些信息，我将编写一项建议，以获取足够的计算资源来完成项目的其余部分。这些模拟的结果将扩展我们对所谓的本质展开蛋白（又称本质上非结构化蛋白）结合其他伴侣蛋白的机制的理解。