BINDING CAPACITY OF THE PDZ2 DOMAIN OF NHERF1

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 摘要利用分子动力学模拟、计算蛋白质修饰和热力学积分方法，我们将集中研究钠/氢交换调节因子1（NHERF 1）的PDZ配体复合物，因为它们具有生物学和医学上的重要性。我们将研究PDZ 2-配体相互作用。为了探测这种相互作用，我们将使用五个氨基酸残基序WETVM（L1）或LFSNL（L2）。我们计划估计PDZ 2对L1和L2的结合亲和力。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Abstract Using Molecular Dynamic (MD) simulations, computational protein modification, and Thermodynamic Integration (TI) method we will concentrate on the studying of the PDZ-ligand complexes of Na/H Exchange Regulatory Factor-1 (NHERF1) due to their biological and medicinal importance. We will investigate the PDZ2-ligand interactions. To probe such interactions we will use the five amino acid residue motifs WETVM (L1) or LFSNL (L2). We are planning to estimate binding affinity of PDZ2 for both L1 and L2.