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首页> 外文学位 >Improved methods of tandem mass spectrometry for proteomics applications in a quadrupole ion trap mass spectrometer.
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Improved methods of tandem mass spectrometry for proteomics applications in a quadrupole ion trap mass spectrometer.

机译：用于四极杆离子阱质谱仪的蛋白质组学应用的串联质谱的改进方法。

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摘要

Tandem mass spectrometry (MS/MS) in the quadrupole ion trap mass spectrometer has become a standard practice for the structural elucidation of peptides for proteomics research. In the quadrupole ion trap mass spectrometer, MS/MS is commonly effected using collision induced dissociation (CID). However, other methods of ion activation, such as infrared multi-photon photodissociation (IRMPD) have been used to dissociate parent ions in the quadrupole ion trap. The process of MS/MS has several limitations resulting from the operation of the quadrupole ion trap mass spectrometer. Two of these limitations are addressed in the research reported in this dissertation.; The first limitation addressed in this research is the loss of structural information resulting from product ions not trapped during the process of CID. During CID in the quadrupole ion trap, product ions with a mass-to-charge approximately one-fourth that of their parent ion's mass-to-charge are not trapped for mass analysis. A method of MS/MS termed High Amplitude Short Time Excitation (HASTE) CID has been developed to allow trapping of these lower mass-to-charge product ions. This method increases the structural elucidation of peptides by providing valuable information in the form of immonium ions that are not mass analyzed using conventional CID methods.; The second limitation to MS/MS addressed in this dissertation is that of dissociating multiple parent ions simultaneously. A method termed Iterative Accumulation Multiplexing (IAM) has been developed to increase the number of ions that can be identified during a single activation event. Using IAM, more than two parent ions can be simultaneously encoded, dissociated, and their resulting product ions identified from a ratiogram. Previous experiments conducted using IAM with CID were limited to a narrow range of qz values for the parent ions. However, other MS/MS techniques such as thermally assisted (TA) CID, IRMPD, and TA-IRMPD, the range of qz values at which a parent ion can be successfully activated during IAM is shown to increase. The increased range of qz values allow more product ions to be identified from the ratiogram, resulting in greater structural elucidation for the peptide parent ions.
机译：四极杆离子阱质谱仪中的串联质谱（MS / MS）已成为蛋白质组学研究用肽的结构阐明的标准方法。在四极离子阱质谱仪中，MS / MS通常使用碰撞诱导解离（CID）进行。但是，其他离子激活方法（例如红外多光子光解离（IRMPD））已用于解离四极离子阱中的母离子。由于四极杆离子阱质谱仪的运行，MS / MS的过程存在一些局限性。本论文报告的研究解决了其中两个局限性。这项研究解决的第一个局限性是CID过程中未捕获的产物离子造成的结构信息损失。在四极杆离子阱的CID期间，质荷比约为其母离子质荷比的四分之一的产物离子不会被俘获用于质量分析。已经开发出一种称为高振幅短时激发（HASTE）CID的MS / MS方法，以捕获这些较低的质荷电荷产物离子。该方法通过以铵离子的形式提供有价值的信息来增加肽的结构阐明，而使用常规CID方法无法对其进行大量分析。本文针对MS / MS的第二个限制是同时解离多个母离子的限制。已经开发出一种称为迭代累积多路复用（IAM）的方法，以增加在单个激活事件中可以识别的离子数量。使用IAM，可以同时对两个以上的母离子进行编码，离解，并从比例图中识别其生成的产物离子。以前使用带有CID的IAM进行的实验仅限于母离子的qz值的狭窄范围。但是，其他MS / MS技术（如热辅助（TA）CID，IRMPD和TA-IRMPD）显示，IAM期间可以成功激活母离子的qz值范围会增加。 qz值范围的增加允许从比例图中识别出更多的产物离子，从而使肽母体离子的结构更清晰。

著录项

  • 作者

    Cunningham, Connell, Jr.;

  • 作者单位

    The University of North Carolina at Chapel Hill.;

  • 授予单位 The University of North Carolina at Chapel Hill.;
  • 学科 Chemistry Analytical.
  • 学位 Ph.D.
  • 年度 2006
  • 页码 182 p.
  • 总页数 182
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;
  • 关键词

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