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Determination and localisation of post translational modifications using Fourier transform ion cyclotron resonance and twodimensional mass spectrometry
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Paris, Johanna (2022) Determination and localisation of post translational modifications using Fourier transform ion cyclotron resonance and twodimensional mass spectrometry. PhD thesis, University of Warwick.
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WRAP_Theses_Paris_2022.pdf - Submitted Version - Requires a PDF viewer. Download (10Mb) | Preview |
Official URL: http://webcat.warwick.ac.uk/record=b3821695
Abstract
Proteins are the building blocks of life; after translation from the genome, they are post translationally modified by enzymes and environmental conditions, which affects their functions, interactions, localisation, and degradation. The characterisation of their post translational modifications (PTMs) is crucial to understand their pivotal role in the regulation, control, and formation of the cellular environment.
The high resolution of mass spectrometry instruments is essential to accurately detect the mass change as a result of a PTM, which could be smaller than one Dalton apart. Tandem mass spectrometry is one of the fundamental methods to localise PTM(s) in proteins and to distinguish between proteoforms. Fragmentation can be performed by the collision of gases, the capture or collision of electrons, and the absorption of photons, through various dissociation mechanisms, giving complementary information on the molecule of interest.
Analysing post translational modifications in complex mixtures such as a proteomics sample is challenging, but possible via data dependant or data independent approaches. The samples are often chemically or enzymatically digested into peptide mixtures, which are separated via liquid chromatography and then analysed in the mass spectrometer. Two-dimensional mass spectrometry (2DMS) is an alternative tool which allows the characterisation of complex mixtures without the need of extensive peptide separations, and isolation of the molecules of interest in the mass spectrometry instrument.
This thesis focuses on the method development and applications of high-resolution mass spectrometry and two-dimensional mass spectrometry in the analysis of proteomics samples and post translational modifications characterisation. Fragmentations of phosphopeptides were achieved with collision gas, electrons, and photons and compared, in a high-resolution instrument. Two-dimensional mass spectrometry applications in the analysis of proteomics samples were developed using the specifics of the 2D technique: the neutral loss lines and the 3D resolution. One of the main breakthroughs of this thesis is the use of 2DMS to detect and localise post translational modifications in complex mixtures.
Item Type: | Thesis (PhD) | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology |
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Library of Congress Subject Headings (LCSH): | Post-translational modification, Proteins -- Chemical modification, Proteomics, Mass spectrometry | ||||
Official Date: | June 2022 | ||||
Dates: |
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Institution: | University of Warwick | ||||
Theses Department: | Department of Chemistry | ||||
Thesis Type: | PhD | ||||
Publication Status: | Unpublished | ||||
Supervisor(s)/Advisor: | O'Connor, Peter B. ; O'Hara, John | ||||
Format of File: | |||||
Extent: | 243 leaves : colour illustrations | ||||
Language: | eng |
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