LTQ MASS SPECTROMETER: STRUCTURAL BIOLOGY

该子项目是利用由NIH/NCRR资助的共享仪器赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。列出的机构是用于资助的，不一定是研究者的机构。描述（申请人提供）：将购买带有电喷雾和MALDI源的Thermo Electron Finnigan LTQ集成离子阱质谱仪、二维液相色谱仪和纳米电喷雾机器人，以满足波士顿大学（BU）医学院和BU Goldman牙科医学院的一组主要用户开展的六个项目的需求。两者都位于BU Medical Campus。这些由NIH资助的研究人员从事（1）确定载脂蛋白B折叠的分子细节（Herscovitz）;（2）N-连接糖基化在下颌下腺发育中的作用（3）硫酸乙酰肝素在血管平滑肌细胞增殖中的作用（Nugent）;（4）淀粉样蛋白疾病中甲状腺素运载蛋白、免疫球蛋白轻链和血清淀粉样蛋白A蛋白的初级和翻译后修饰结构（Skinner）;（5）核心蛋白聚糖在角膜生物化学中的作用（Trinkaus-Randall）;（6）确定与生长因子结合的糖胺聚糖的结构（Zaia）。一组五个小用户，四个来自BU医学校园，一个来自纽约大学医学院，需要最先进的离子阱质谱法来支持牙周宿主-寄生虫相互作用的研究（Amar）;骨桥蛋白的翻译后（Berman）; C。elegans N-糖基化（Hirschberg）;小窝的蛋白质和脂质组分的研究（Pilch）;和uroplakins的N-糖基化的分析（Sun）。集成的LTQ离子阱质谱系统将被安置在BUSM共享质谱仪器实验室。优先考虑所描述的项目;小用户以及更大的BUSM社区将在剩余的时间内提供服务。 仪器将由有经验的人员操作和维护。仪器操作、用品和服务合同的费用将由用户分摊，如他们的支持信中所述。仪器操作员的工资将由BU医学院院长提供。

This subproject is one of many research subprojects utilizing the resources provided by a Shared Instrumentation 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 grant, which is not necessarily the institution for the investigator. DESCRIPTION (provided by applicant): A Thermo Electron Finnigan LTQ integrated ion trap mass spectrometer with electrospray and MALDI sources, a two-dimensional liquid chromatograph, and a nano-electrospray robot will be purchased to meet the needs of six projects that are carried out by a group of major users based at Boston University (BU) School of Medicine and BU Goldman School of Dental Medicine, both located on the BU Medical Campus. These NIH-funded investigators are engaged in (1) determining the molecular details of the folding of apolipoprotein B (Herscovitz); (2) the role of N-linked glycosylation in submandibular gland development (Kukuruzinska); (3) the role of heparan sulfates in vascular smooth muscle cell proliferation (Nugent); (4) the primary and post-trranslational modification structures of transthyretin, immunoglobulin light chains, and serum amyloid A protein in amyloid diseases (Skinner); (5) the role of decorins in corneal biochemistry (Trinkaus-Randall); (6) determination of the structures of glycosaminoglycans that bind to growth factors (Zaia). A group of five minor users, four from the BU Medical Campus and one from New York University School of Medicine, have need for state-of-the-art ion trap mass spectrometry to support studies of periodontal host-parasite interactions (Amar); post-translations to osteopontin (Berman); C. elegans N- glycosylation (Hirschberg); studies of the protein and lipid components of caveolae (Pilch); and analysis of the N-glycosylation of uroplakins (Sun). The integrated LTQ ion trap mass spectrometry system will be housed in the BUSM Shared Mass Spectrometry Instrumentation Laboratory. Priority will be given to the projects described; minor users as well as the larger BUSM community will be served in the remaining time. The instrument will be operated and maintained by experienced personnel. The costs of instrument operation, supplies, and service contract will be shared by the users, as stated in their support letters. The salary for the instrument operator will be provided by the Dean of BU School of Medicine.