Mass Spectrometry Of Drugs, Natural Products, Proteins,

在过去的一年里，这个单位的研究几乎完全转向蛋白质组研究。该小组确定了二硫键和蛋白质中的其他翻译后修饰，这是合作研究的一部分。方法的改进和发展是该小组重点关注的重要方面。在过去的一年里，实验室购买了一台新的Q-TOF质谱仪，这是NIDDK和其他四个研究所合作购买的。其使用由合作研究所共享。仪器和数据的预订都可以在线获得，因此远程研究人员可以处理他们的数据，并且只需到实验室插入他们的样本。这种资源共享被证明是非常成功的。还增加了凝胶消化站，用于更大规模的消化和鉴定在正常和患病状态之间丰度不同的蛋白质。虽然使用凝胶来识别这些蛋白质是一种有用的方法，但该小组开发工作的重点是对细胞系统的整个蛋白质组进行这些分析的方法。该小组的主要研究项目包括确定非常大和复杂的蛋白质中的翻译后修饰，疏水蛋白质的分析和鉴定方法，生物活性肽中不寻常/修饰氨基酸的鉴定，开发交联方法以阐明蛋白质的3-D结构和蛋白质相互作用，新型膜联蛋白的表征，以及鉴定S-腺苷甲硫氨酸脱羧酶的体内修饰。与生物物理化学实验室（NHLBI）保持着非常密切的合作。

The research of this unit has moved over the last year to almost entirely proteome research. The group identifies disulfide bonds and other post-translational modifications in proteins that are part of collaborative research. Method improvement and development are important aspects of the group's emphasis. Over the past year, a new Q-TOF mass spectrometer has been acquired by the laboratory and this was a collaborative purchase between NIDDK and four other institutes. Its use is shared between the collaborating institutes. Booking for the instrument and the data are all made available online so the remote researchers can process their data and must only come to the laboratory to insert their samples. This is sharing of the resource is proving highly successful. A gel digestion station was also added for larger scale digestion and identification of proteins that vary in abundance between a normal and diseased state. While using gels to identify these proteins is a useful approach, an emphasis in the group's development work has been in methods for doing these analyses on the whole proteome from a cell system. Major research projects within the group have involved the determination of post-translational modifications in very large and complex proteins, methods for the analysis and identification of hydrophobic proteins, the identification of unusual/modified amino acids in biologically active peptides, development of cross-linking method to elucidate 3-D structures of proteins and proteins interactions, the characterization of novel annexins, and the identification of an in-vivo modification of S-adenosylmethionine decarboxylases. A very close collaboration is maintained with the Laboratory of Biophysical Chemistry, NHLBI.