Legacy Support During Closure of the Mass Spectrometry Resource for Biology and Medicine

波士顿大学生物学和医学质谱资源的使命是 开发和应用先进的，基于质谱的方法， 表征与人类健康和疾病相关的生物聚合物。其稳定 基础科学家、临床医生、 和实习生。由于NIGMS现在对P41赠款规定了时间限制， GM 104603无法续订。该提案要求提供必要的资金，以避免 资源活动的突然中断，并提供平稳的过渡期 使正在进行的生物医学和合作项目能够有序完成， 依赖于资源中唯一可用的方法和专业知识，完成正在进行的 软件开发，共享软件，数据库和协议，以满足 以及确定和实施替代机制， 用户社区的未来需求，并使进一步的技术发展， 从过去20年资源的成就演变而来。该资源将 专注于糖生物学的需要，详细的结构解析和分析， 聚糖的复杂混合物。阐明聚糖裂解途径的参考数据 使用多种解离方法的研究结果将被汇编并存入公共数据库; 新的，用户友好的生物信息学工具，资源正在创建的聚糖分析将 完成，测试和共享。离子迁移率-串联的方案和参考数据集 质谱法将被编译用于聚糖和复杂肽混合物的分析， 用于表征非共价复合物，并用于评估新的ExD细胞设计， 由一个小型工业合作者建造。内部开发的聚糖软件 变体和后修饰结构确定和自上而下的分析 将完成能够在单个蛋白质上的PTM之间建立关系的蛋白质 和共享;它应该提供直接的临床分析手段， 蛋白质-聚糖和蛋白质-蛋白质相互作用。待完成的翻译项目将 包括N-和O-连接聚糖和脂多糖对感染性 细菌和寄生虫中糖脂和糖胺聚糖的结构测定 人乳、蛋白质错误折叠病症、免疫学、细胞外基质生物学和 心血管疾病该资源将转让其在培训学生方面的经验， 博士后研究员和实践科学家到其他教育机构和行业。

The mission of the Boston University Mass Spectrometry Resource for Biology and Medicine is the development and application of advanced, mass spectrometry-based methods for the characterization of biopolymers that are relevant to human health and disease. Its steady progress has been fostered by close working relationships between basic scientists, clinicians and trainees. Because NIGMS has now imposed a time limit for P41 grants, the grant P41 GM104603 cannot be renewed. This proposal requests the funding essential to avoid a disruptive sudden closedown of the Resource's activities and afford a smooth transition period to enable the orderly completion of ongoing driving biomedical and collaborative projects that depend on methods and expertise uniquely available in the Resource, finalizing of ongoing software development, sharing of software, databases and protocols to meet the needs of the community, and the identification and implementation of alternative mechanisms to address the future needs of the user community and enable further technology developments that should evolve from the accomplishments of the Resource over the last 20 years. The Resource will focus on the needs of glycobiology for detailed structural elucidations and the profiling of complex mixtures of glycans. Reference data that illuminates glycan fragmentation pathways using multiple dissociation methods will be compiled and deposited into public databases; the new, user-friendly bioinformatics tools that the Resource is creating for glycan analysis will be completed, tested and shared. Protocols and sets of reference data for Ion mobility-tandem mass spectrometry will be compiled for the analysis of glycans and complex peptide mixtures, for characterization of noncovalent complexes, and for evaluation of new ExD cell designs being constructed by a small industry collaborator. In-house in developed software for glycan structural determinations and top-down analysis of variant and post-translationally modified proteins, that can establish relationships among PTMs on individual proteins, will be completed and shared; it should provide means for straightforward clinical analyses, and for probing protein-glycan and protein-protein interactions. Translational projects to be completed will include characterization of N- and O-linked glycans and lipopolysaccharides on infectious bacteria and parasites, structural determinations of glycolipids and glycosaminoglycans in human milk, protein misfolding disorders, immunology, extracellular matrix biology and cardiovascular disease. The Resource will transfer its experience in training students, postdoctoral fellows and practicing scientists to other educational institutions and industry.