LTQ MASS SPECTROMETER: STRUCTURAL BIOLOGY

这个子项目是利用由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。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是用于拨款的，而不一定是用于调查人员的机构。描述(由申请人提供)：将购买一台集成了电喷雾和MALDI源的Thermo Electron Finnigan LTQ离子陷阱质谱仪、一台二维液相色谱仪和一台纳米电喷雾机器人，以满足波士顿大学医学院和波士顿大学高盛牙医学院的一组主要用户实施的六个项目的需求，这两个项目都位于波士顿大学医学院。这些由美国国立卫生研究院资助的研究人员从事以下工作：(1)测定载脂蛋白B折叠的分子细节(赫斯科维茨)；(2)N-连接糖基化在颌下腺发育中的作用(Kukuruzinska)；(3)硫酸乙酰肝素在血管平滑肌细胞增殖中的作用(Nugent)；(4)转甲状腺素、免疫球蛋白轻链和血清淀粉样蛋白A在淀粉样疾病中的初级和翻译后修饰结构(Skinner)；(5)核心蛋白在角膜生化中的作用(Trinkaus-Randall)；(6)测定与生长因子结合的糖胺聚糖的结构(ZAIA)。一个由五名小使用者组成的小组，四名来自波士顿大学医学院，一名来自纽约大学医学院，需要最先进的离子陷阱质谱仪来支持牙周宿主-寄生虫相互作用(AMAR)的研究；翻译成骨桥蛋白的后翻译(Berman)；秀丽隐杆菌的N-糖基化(Hirschberg)；小凹的蛋白质和脂肪成分的研究(PILCH)；以及尿板N-糖基化的分析(SUN)。集成的LTQ离子陷阱质谱仪系统将安装在北京邮电大学共用的质谱仪实验室。将优先考虑所描述的项目；在剩余时间内，将为较小的用户以及较大的BUSM社区提供服务。仪器将由经验丰富的人员操作和维护。仪器操作、供应和服务合同的费用将由用户分担，如他们的支持信中所述。仪器操作员的工资将由北京大学医学院院长提供。

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.