MRI: Acquisition of a Mass Spectrometer to Enable Research and Education at the Interface of Chemistry, Biology, and Materials Science

匹兹堡大学的William Horne教授及其同事Tara Meyer和Alexander Deiters获得了来自主要研究仪器(MRI)和化学研究仪器和设施(CRIF)计划的这一奖项，从而获得了一台基质辅助激光解吸/电离飞行时间质谱仪(MALDI-TOF/TOF MS)。通常，质谱学是用于识别和表征嵌入在复杂基质中的少量化学物种的关键分析方法之一。激光照射到嵌入样品的惰性基质上，使样品汽化和电离。离子进入质谱仪，在那里测量母离子和碎片离子的质量。在飞行时间仪器中，离子被电场加速，以进行进一步的表征。MALDI TOF将温和的电离(非常适合生产完整的多肽、蛋白质、核酸、碳水化合物、合成聚合物和其他类似大小物种的离子)与检测模式相结合，在广泛的质量范围内提供了灵敏度和准确性之间的极佳平衡。这种高度灵敏的技术可以识别和确定复杂混合物中的分子结构。此次收购加强了该大学和该地区的研究基础设施。该仪器通过让不同的学生参与这一现代分析技术的研究和研究培训，扩大了参与。该奖项旨在加强各级的研究和教育，特别是在下列领域的研究和教育：(A)构建结构定义的超分子生物材料；(B)制定设计复杂蛋白质折叠模式的生物稳定模拟物的策略；(C)深入了解序列在决定聚合物性质中的基本作用；(D)探索对生物系统中合成寡核苷酸进行小分子调控的方法；以及(E)开发超出20种典型氨基酸的定点蛋白质突变的方法。

With this award from the Major Research Instrumentation (MRI) and Chemistry Research Instrumentation and Facilities (CRIF) programs, Professor William Horne from the University of Pittsburgh and colleagues Tara Meyer and Alexander Deiters have acquired a matrix assisted laser desorption/ionization time-of-flight mass spectrometer (MALDI-TOF/TOF MS). In general, mass spectrometry is one of the key analytical methods used to identify and characterize small quantities of chemical species embedded in complex matrices. A laser impinging on the inert matrix embedded with the sample, vaporizes and ionizes the sample. The ions pass into the mass spectrometer where the masses of the parent ion and its fragment ions are measured. In a time-of-flight instrument the ions are accelerated by an electric field to allow further characterization. MALDI TOF combines gentle ionization (ideal for producing intact ions of peptides, proteins, nucleic acids, carbohydrates, synthetic polymers, and other similarly sized species) with a detection mode that offers an excellent balance between sensitivity and accuracy across a wide mass range. This highly sensitive technique allows identification and determination of the structure of molecules in a complex mixture. The acquisition strengthens the research infrastructure at the University and regional area. The instrument broadens participation by involving diverse students in research and research training with this modern analytical technique.The award is aimed at enhancing research and education at all levels, especially in areas such as (a) constructing structurally defined supramolecular biomaterials; (b) developing strategies for designing biostable mimics of complex protein folding patterns; (c) providing insights into the fundamental role of sequence in dictating polymer properties; (d) searching for approaches for small-molecule regulation of synthetic oligonucleotides in biological systems and (e) developing methods for site-specific protein mutagenesis that expand beyond the 20 canonical amino acids.