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.

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