University of Illinois Urbana-Champaign

Design of the First Analytical Platform for Automated Top Down Proteomics With quadrupole/Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Patrie, Steven M.

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https://hdl.handle.net/2142/84159

Description

Title
Design of the First Analytical Platform for Automated Top Down Proteomics With quadrupole/Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
Author(s)
Patrie, Steven M.
Issue Date
2004
Doctoral Committee Chair(s)
Kelleher, Neil L.
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
Abstract
The enclosed writing details technology development leading to the first high-throughput proteome analysis of Methanosarcina acetivorans utilizing a custom FT mass spectrometer. It outlines a two dimensional separations platform that utilizes a 96 well plate nanospray robot to facilitate automated analysis on the mass spectrometer. This thesis also highlights instrument advancements required to improve throughput for observation of protein intact masses and methods used to obtain robust fragmentation. Included within the automation platform is software developed for efficiently managing intact protein and MS/MS data. Also, a novel fragmentation method has been developed to extend dynamic range for fragmentation of intact proteins as large as 60 kDa. The enclosed work is the foundation for the first fully automated platform for intact protein analysis by tandem MS. With the identification of hundreds of proteins from a single run, the high-throughput Top Down proteome analysis of intact proteins is now a reality.
Graduation Semester
2004
Type of Resource
text
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http://hdl.handle.net/2142/84159

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