LD FTMS OF HIGH MASS BIOMOLECULES

要求提供支助，以继续调查 傅里叶变换质谱法分析非挥发性 质量在2，000至100，000道尔顿范围内的生物分子，或 高研究的一个原则重点将是进一步发展 高分辨率基质辅助激光解吸新技术 （MALDI）允许其应用于以前的生物分析问题 无法通过质谱法进行研究。研究将利用 Extrel 7.2 Tesla FTMS双池仪器和3 Tesla尼科莱FTMS- 1000台单细胞仪器最近被改装为激光解吸 操作有待探讨的工具和方法的发展 包括：研究一种新5板门控捕获程序， 在MALDI应用中;检查新的激光解吸几何形状， 解吸物质垂直于磁场，而不是平行于磁场 高质量离子四极轴向化的发展 与MALDI结合;增加了高性能快速切换 用于轴向化和表面诱导的捕获模块 解离实验样品制备和分析应用 研究将：进一步研究混合MALDI矩阵的使用， 基质成分对大分子MALDI的影响;研究 用于产生多电荷离子的样品制备方法， MALDI，目标是实现一些质量范围和分辨率 将允许的优势;探索MALDI-FTMS的应用， 蛋白质以外的化合物种类，如核苷酸， 核苷和寡糖;以及改进的离线MALDI方法 毛细管电泳流出物。 MALDI的基本原理也将进行研究，目的是了解 控制这个过程的因素。这些研究预计将 在设计有效的新技术方面提供实质性援助， 生物分析应用。

Support is requested for continued investigations of applications of Fourier transform mass spectrometry to analysis of non-volatile biomolecules with masses in the range of 2,000 to 100,000 daltons or higher. A principle emphasis of the research will be further development of the new technique of high resolution matrix-assisted laser desorption (MALDI) to allow its application to bioanalytical problems previously impossible to investigate by mass spectrometry. The research will utilize an Extrel 7.2 Tesla FTMS dual cell instrument and a 3 Tesla Nicolet FTMS- 1000 single cell instrument recently converted for laser desorption operation. Instrumental and methodological developments to be explored include: investigation of a new 5-plate gated trapping procedure for use in MALDI applications; examination of a new laser desorption geometry, desorbing materials normal, rather than parallel, to the magnetic field axis; development of quadripolar axialization of high mass ions in conjunction with MALDI; addition of a high performance rapid switching trapping module for use in both axialization and surface-induced dissociation experiments. Sample-preparation and analytical application studies will: further examine the use of mixed MALDI matrices and the effects of matrix composition on MALDI of high mass molecules; investigate sample preparation methods intended to produce multiply-charged ions by MALDI, with the goal of achieving some of the mass range and resolution advantages that would allow; explore application of MALDI-FTMS to categories of compounds other than proteins, such as nucleotides, nucleosides, and oligosaccharides; and improve methods for off-line MALDI of capillary electrophoresis effluents. Fundamentals of MALDI also will be studied with the aim of understanding the factors governing the process. These studies are expected to be of substantial assistance in designing efficacious new techniques for bioanalytical applications.