Wei, Juan (2014) Advanced applications of high performance Fourier transform ion cyclotron resonance mass spectrometry. PhD thesis, University of Warwick.

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Abstract

Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) displays its advances in obtaining high resolving power, high mass accuracy, and coupling with many different tandem mass spectrometry (MS/MS) techniques. In this thesis, the superior performance of FTICR MS was demonstrated by several different applications. The peak separation limit of the 12 T solariX FTICR instrument was challenged by measuring the isotopic fine structures of several 17O enriched amyloid-β (Aβ) peptides (Chapter 2 and 3). A resolving power as high as 6 M was achieved at m/z 880, and peaks were assigned with mass uncertainty less than 70 ppb. The accurate measurement of 17O labelling ratio is of value for estimating atomic distances by NMR experiments. Furthermore high mass accuracy and high resolution are proved vital for the confident assignment of peaks in a polymeric mixture due to the sample complexity and coexistence of different adducts (Chapter 4). On the other hand, one or more of the MS/MS techniques, collisionally activated dissociation (CAD), electron induced dissociation (EID), electron capture dissociation (ECD), and infrared multiphoton dissociation (IRMPD), were used to characterize the structures of chlorophyll-a (Chapter 6), pheophytin-a (Chapter 7), and d-α-tocopheryl polyethylene glycol succinate (TPGS), repectively, and diagnostic fragments are useful for their structural identification in the future. IRMPD was particularly efficient in fragmenting chlorophyll-a and pheophytin-a compared to EID and CAD. Based on the fragmentation pattern of TPGS attached with two different adducts (Li+, Na+, K+, Ag+, and H+), investigating the influence of adducts in ECD and CAD processes are of benefit for understanding the fragmentation mechanisms when cation adducts are involved (Chapter 5). In an on-going project, FTICR also displays the capability to study intact proteins above 30 kDa (Chapter 8).

Item Type:	Thesis or Dissertation (PhD)
Subjects:	Q Science > QD Chemistry
Library of Congress Subject Headings (LCSH):	Ion cyclotron resonance spectrometry, Fourier transform spectroscopy
Official Date:	August 2014
Dates:	Date Event August 2014 Submitted
Institution:	University of Warwick
Theses Department:	Department of Chemistry
Thesis Type:	PhD
Publication Status:	Unpublished
Supervisor(s)/Advisor:	O'Connor, Peter B.
Sponsors:	University of Warwick ; University of Warwick. Department of Chemistry
Extent:	xix, 281 leaves : charts
Language:	eng

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