Addition of Tandem Mass Spectrometry to the Middle Atlantic Mass Spectrometry Facility for the Analysis of Complex Biomolecules

这是一个生物设施中心的请求， 购买和开发支持串联质谱仪， 或MS/MS，用作共享仪器设施， 中大西洋质谱仪的一部分 该仪器，将位于巴尔的摩县校园， 马里兰州大学将补充现有的 美国约翰霍普金斯大学的MAMS实验室所具备的能力 大学 主要研究者的核心和合作研究 他们的工作人员将包括仪器开发和 应用于复杂生物分子的分析。 仪器 发展将集中在提高碎片离子的产率 利用碰撞和激光获得大分子的信息 在MS 1和MS 2之间的field.free区域中的光解离。 将采用多次碰撞来诱导 碎片化，中和分子和碎片离子， 平衡离子动能和内能。 碎片离子将 然后通过化学电离来重新电离并允许二次B 在第二质谱仪中以高于 通常用于high.energy冲突的B/E扫描。 MS/MS将用于诱导结构断裂，改善 样品离子信号相对于基质离子，区分 由几种分子离子种类形成的碎片离子，以及 微观非均相和其他混合物的单独组分， 易于通过液相色谱技术分离。 这些 将利用其优势进行结构分析 糖肽，脂多糖，化学和后。 修饰的肽、合成核苷酸等， 正在进行的合作项目在设施。

This is a Biological Facilities Center request for the purchase and developmental support of a tandem mass spectrometer, or MS/MS, to be used as a shared instrumental facility and as part of the Middle Atlantic Mass Spectrometry Facility. The instrument, to be located on the Baltimore County campus of the University of Maryland, will supplement existing capabilities available at the MAMS Facility at the Johns Hopkins University. Core and collaborative research by the principal investigators and their staff will include both instrument development and applications to the analysis of complex biomolecules. Instrument development will focus on improving the yield of fragment ion information for larger molecules using both collisions and laser photodissociation in the field.free region between MSl and MS2. Multiple collisions will be employed to induce fragmentation,neutralize molecular and fragment ions and equilibrate ion kinetic and internal energy. Fragment ions will then bereionized by chemical ionization and permit quadratic B scans in the second mass spectrometer at higher resolution than the B/Escans normally employed for high.energy collisions. MS/MS will be used to induce structural fragmentation, improve the sample ion signal relative to matrix ions, distinguish fragment ions formed from several molecular ion species, and separate components of microheterogeneous and other mixtures not readily separable by liquid chromatographic techniques. These advantages will be exploited for the structural analyses ofglycopeptides, lipopolysaccharides, chemically and post. translationally modified peptides, synthetic nucleotides, etc. in ongoing collaborative projects at the facility.