CHARACTERIZING THE CONFORMATIONAL PREFERENCES OF P53 PEPTIDES

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。子项目和 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。 在接下来的几个月中，我将使用 Teragrid 上 30,000 个服务单元 (SU) 的开发分配来进行分子动力学模拟，以原子细节表征 (TAD) 肿瘤抑制因子 p53 的天然未折叠转录激活结构域的肽片段的构象偏好。虽然此开发分配不足以让我执行所有必需的模拟，但我能够运行的模拟将为估计我在 Teragrid 上的剩余计算需求提供有用的信息。考虑到这些信息，我将编写一份提案，以获得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天然未折叠蛋白质（又称本质上非结构化蛋白质）与其他伙伴蛋白质结合的机制的理解。

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.