THE EFFECT OF ?-SYNUCLEIN ON MEMBRANE STRUCTURE

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。 ?-突触核蛋白由于其在帕金森病中形成纤维状聚集体的倾向及其未知的功能性而仍然是感兴趣的蛋白质。?-突触核蛋白定位于突触囊泡，其相对较小，直径约为40 nm。 由于这种小尺寸，组分脂质处于曲率应力下，该应力通过融合而减轻。 我们假设？-突触核蛋白通过缓解这种弯曲应力来调节突触囊泡融合。使用全原子分子动力学模拟，我们将研究的结构？- Synuclein  膜复合物和蛋白质结合对膜曲率的影响。

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. ?-Synuclein remains a protein of interest due to its propensity to form fibrillar aggregates in Parkinson's Disease and its unknown functionality. ?-Synuclein localizes to synaptic vesicles, which are relatively small, with diameters of ~40 nm. Because of this small size the component lipids are under a curvature stress, which is relieved by fusion. We hypothesize that ?-Synuclein regulates synaptic vesicle fusion by relieving this curvature stress. Using all-atom molecular dynamics simulations we will examine the structure of ?-Synuclein  membrane complexes and the affect of protein binding on membrane curvature.