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

这是一份生物设施中心的购买和开发支持串联质谱仪（MS/MS）的请求，该串联质谱仪将用作共享仪器设备，并作为中大西洋质谱仪设备的一部分。该仪器将位于马里兰大学巴尔的摩校区，将补充约翰霍普金斯大学MAMS设施的现有能力。主要研究人员及其工作人员的核心和合作研究将包括仪器开发和复杂生物分子分析的应用。仪器的开发将集中在利用ms1和MS2之间的场自由区域的碰撞和激光光解作用来提高大分子碎片离子信息的产量。多重碰撞将被用来诱导碎片化，中和分子和碎片离子，平衡离子动力学和内能。然后，碎片离子将被化学电离，并允许在第二个质谱仪中进行二次B扫描，其分辨率比通常用于高分辨率的B/ escan更高。能量碰撞。MS/MS将用于诱导结构破碎，改善样品离子相对于基质离子的信号，区分由几种分子离子形成的碎片离子，以及分离液相色谱技术难以分离的微异质组分和其他混合物。这些优点将被用于糖肽、脂多糖的结构分析、化学分析和后期分析。翻译修饰肽，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.