Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.635611
Title: Advanced applications of high performance Fourier transform ion cyclotron resonance mass spectrometry
Author: Wei, Juan
ISNI:       0000 0004 5357 7313
Awarding Body: University of Warwick
Current Institution: University of Warwick
Date of Award: 2014
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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).
Supervisor: Not available Sponsor: University of Warwick
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.635611  DOI: Not available
Keywords: QD Chemistry
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