ESI Q-TOF Mass Spectrometer with UHPLC

在慕尼黑工业大学（TUM）的生物分子和生物医学研究框架内，蛋白质既作为研究对象-关于生物催化或受体结合活性以及结构分析-又作为细胞生物学、生物医学和动物实验中的生物活性试剂。为此，需要高纯度且生物化学精确表征的蛋白质制剂，而电喷雾电离质谱（ESI-MS）为完整蛋白质的分子组成提供最终且有据可查的证据。ESI-MS提供了必要的信息，既可以确认遗传编码的突变（作为自然变异或蛋白质工程的结果），也可以识别翻译后修饰，这可能取决于宿主生物体。在这种情况下，蛋白质组学方法的价值有限，因为基于肽的质谱法仅提供关于多肽的分离片段的信息。只有通过适当配备的ESI-MS仪器才能深入了解蛋白质的完整组成或甚至蛋白质制剂的均匀性（通过直接进样而无需预先进行色谱分离），该仪器甚至允许在适当的测量条件下分析蛋白质和分子相互作用伴侣（金属离子，小分子配体，核酸，其他蛋白质）之间的复合物。这些数据今天通常需要在著名的科学期刊上发表，也有助于在动物研究以及转化生物医学研究中应用蛋白质的质量控制。由于TUM生命科学校区魏亨斯特潘的一台使用了10年的仪器在最近制造商维护到期后将很快面临停止使用，因此需要根据当前技术状况配备一台新的ESI Q-TOF质谱仪（配备UHPLC）。这项投资一方面将为TUM在蛋白质科学领域的国际竞争力研究提供未来的仪器基础，特别是在蛋白质工程和设计领域，包括其与非天然氨基酸的共翻译结合的进步;另一方面，TUM的这一独特仪器将促进国际水平的生命科学研究，不仅在魏亨斯特潘生命科学学院以及慕尼黑大学的其他学院，而且在与慕尼黑大学医院rechts der Isar（MRI）的多个合作框架内。专业的操作和用户的广泛访问将通过与巴伐利亚生物分子质谱中心（BayBioMS）在校园魏亨斯特潘的附属关系得到保证。

In frame of the biomolecular and biomedical research at the Technical University of Munich (TUM) proteins serve both as research subjects – with regard to biocatalytic or receptor binding activities as well as structural analysis – and as bioactive reagents in cell biology, biomedicine and animal experiments. To this end, highly pure and biochemically precisely characterized protein preparations are needed while electrospray ionization mass spectrometry (ESI-MS) provides final and well documented proof of the molecular composition of the intact protein. ESI-MS offers essential information, both to confirm genetically encoded mutations (either as natural variations or as result of protein engineering) and to identify posttranslational modifications, which may vary depending on the host organism. In this context, proteomics methods are of limited value since peptide-based mass spectrometry just provides infomation about isolated segments of a polypeptide. Insight into the complete composition of a protein or even the homogeneity of a protein preparation (as measured by direct injection without previous chromatographic fractionation) is only available by means of a suitably equipped ESI-MS instrument, which even allows the analysis of complexes between proteins and molecular interaction partners (metal ions, small molecule ligands, nucleic acids, other proteins) under appropriate measurement conditions. Such data are generally required today for publications in renowned scientific journals and are also instrumental as quality control for the application of proteins in animal studies as well as in translational biomedical research. Since a 10 year-old instrument at the life science campus Weihenstephan of TUM will soon face cease of use after the recent expiry of the manufacturer's maintenance, a new ESI Q-TOF mass spectrometer with UHPLC according to the current state of technology is requested. This investment will, on the one hand, provide the future instrumentation basis for internationally competitive research at TUM in protein science, especially in the area protein engineering & design and including its advancement with the cotranslational incorporation of non-natural amno acids; on the other hand, this unique instrument at TUM will boost research in the life sciences at international level, not only at the School of Life Sciences in Weihenstephan as well as other Schools of TUM but also in the frame of multiple collaborations with the Munich University Hospital rechts der Isar (MRI). The professional operation and broad access by users will be guaranteed via affiliation with the Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) at the Campus Weihenstephan.