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首页> 外文学位 >Gaining insight into electron capture dissociation mass spectrometry of peptides and proteins.
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Gaining insight into electron capture dissociation mass spectrometry of peptides and proteins.

机译：深入了解肽和蛋白质的电子捕获解离质谱。

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摘要

The study of protein structure is crucial to the understanding of protein function as the two are inter-dependent. Protein structure analysis is especially important as misfolded proteins often result in fatal diseases. Gas-phase protein structure analysis provides a way to study the forces the effects of solvent and involved in the determination of protein structure. Mass spectrometry (MS) is a rapid and sensitive technique that can be used for the analysis of gas-phase protein structure.;Electron capture dissociation (ECD) tandem mass spectrometry (MS/MS) has been used in the analysis of primary, secondary, and tertiary gas-phase protein structure. ECD-MS/MS has proved to be exceptionally applicable in the study of protein structure due to the ability to cleave protein backbone bonds with the retention of noncovalent interactions and small-molecule post-translational modifications. The work described in this dissertation expands the use ECD and other electron capture techniques for protein structure analysis.;All of the experiments were performed using a unique and versatile hybrid linear ion trap/time-of-flight (LIT/TOF) mass spectrometer capable of multiple ion activation techniques, such as collision induced dissociation (CID), infrared multiphoton dissociation (IRMPD), ECD, hot ECD (HECD), and activated-ion ECD (AI-ECD). IR activation in conjunction with ECD (AI-ECD) to disrupt noncovalent interactions was used to enhance primary structure analysis and monitor changes in tertiary structure via gas-phase protein unfolding. The structure of the z·-type product ions was probed using ion-molecule reactions, and the formation different structures was found to depend on the electron capture technique used to dissociate the parent ion.;The work described in this dissertation demonstrates the use of AI-ECD for analysis of gas-phase protein structure. Also, the first analysis of z ·-ion structure from various electron capture techniques is presented. This work highlights the versatility and utility of the LIT-TOF for ECD-MS/MS as an alternative to the commercial Fourier transform ion cyclotron resonance (FTICR) mass spectrometers.
机译：蛋白质结构的研究对于理解蛋白质功能至关重要，因为两者是相互依赖的。蛋白质结构分析尤其重要，因为错误折叠的蛋白质通常会导致致命的疾病。气相蛋白质结构分析提供了一种方法来研究作用力对溶剂的影响并参与蛋白质结构的确定。质谱（MS）是一种快速灵敏的技术，可用于分析气相蛋白质结构。;电子捕获解离（ECD）串联质谱（MS / MS）已用于一级，二级分析和三级气相蛋白质结构。 ECD-MS / MS被证明在蛋白质结构研究中格外适用，因为它具有裂解蛋白质主链键的能力，同时保留了非共价相互作用和小分子翻译后修饰。本文所描述的工作扩展了ECD和其他电子捕获技术在蛋白质结构分析中的应用。所有实验均使用独特且通用的混合线性离子阱/飞行时间（LIT / TOF）质谱仪进行多种离子活化技术，例如碰撞诱导解离（CID），红外多光子解离（IRMPD），ECD，热ECD（HECD）和活化离子ECD（AI-ECD）。红外激活结合ECD（AI-ECD）来破坏非共价相互作用被用于增强一级结构分析并通过气相蛋白展开监测三级结构的变化。利用离子分子反应对z·型产物离子的结构进行了研究，发现形成不同的结构取决于用于解离母离子的电子捕获技术。 AI-ECD用于分析气相蛋白质结构。此外，提出了从各种电子捕获技术对z·离子结构的首次分析。这项工作强调了LIT-TOF在ECD-MS / MS方面的多功能性和实用性，可替代商用傅里叶变换离子回旋共振（FTICR）质谱仪。

著录项

  • 作者

    Thompson, Natalie J.;

  • 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.;Chemistry Biochemistry.
  • 学位 Ph.D.
  • 年度 2010
  • 页码 144 p.
  • 总页数 144
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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