CHARACTERIZING THE CONFORMATIONAL PREFERENCES OF P53 PEPTIDES

这个子项目是许多利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 在接下来的几个月里，我将使用我在Teragrid上分配的30，000个服务单位（SU）进行分子动力学模拟，以原子细节表征肿瘤抑制因子p53的天然未折叠转录激活结构域的肽片段的构象偏好。虽然这个开发分配不足以让我执行所有所需的模拟，但我将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。有了这些信息，我将写一份提案，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大我们对所谓的天然未折叠蛋白质（又名蛋白质）的机制的理解。本质上非结构化的蛋白质与其他伴侣蛋白质结合。

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.