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Porcine P2 myelin protein primary structure and bound fatty acids determined by mass spectrometry
Stockholm University, Faculty of Science, Department of Analytical Chemistry.
Stockholm University, Faculty of Science, Department of Analytical Chemistry.
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2010 (English)In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 397, no 5, 1903-1910 p.Article in journal (Refereed) Published
Abstract [en]

Complementary collision-induced/electron capture dissociation Fourier-transform ion cyclotron resonance mass spectrometry was used to fully sequence the protein P2 myelin basic protein. It is an antigenic fatty-acid-binding protein that can induce experimental autoimmune neuritis: an animal model of Guillain-Barre syndrome, a disorder similar in etiology to multiple sclerosis. Neither the primary structure of the porcine variant, nor the fatty acids bound by the protein have been well established to date. A 1.8-angstrom crystal structure shows but a bound ligand could not be unequivocally identified. A protocol for ligand extraction from protein crystals has been developed with subsequent gas chromatography MS analysis allowing determination that oleic, stearic, and palmitic fatty acids are associated with the protein. The results provide unique and general evidence of the utility of mass spectrometry for characterizing proteins from natural sources and generating biochemical information that may facilitate attempts to elucidate the causes for disorders such as demyelination.

Place, publisher, year, edition, pages
2010. Vol. 397, no 5, 1903-1910 p.
Keyword [en]
CID, ECD, De novo sequencing, GC/MS, Lipid identification, Myelin proteins
National Category
Analytical Chemistry
Identifiers
URN: urn:nbn:se:su:diva-50527DOI: 10.1007/s00216-010-3762-0ISI: 000278810000032OAI: oai:DiVA.org:su-50527DiVA: diva2:381624
Note
authorCount :8Available from: 2010-12-28 Created: 2010-12-28 Last updated: 2017-12-11Bibliographically approved
In thesis
1. Strategies to explore the membrane proteome of a cell
Open this publication in new window or tab >>Strategies to explore the membrane proteome of a cell
2011 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The cell envelope plays key roles in numerous processes such as maintaining cellular integrity, communication with other cells, signal transduction, maintenance of cellular homeostasis, and regulation of the traffic of molecules between the cell and the extracellular milieu. Essential membrane components in many of these processes are proteins. It is estimated that ~20-30% of the predicted open reading frames (ORFs) of all organisms encode membrane proteins. Furthermore, two thirds of drug targets are membrane proteins. However, despite their importance, membrane proteins have so far been mostly neglected in most proteomic studies, due to the inherent challenges in analyzing them.

The focus of this thesis is to devise strategies that allow investigation of membrane proteins and their associated complexes. Optimization of sample preparation in the underlying studies has allowed important goals to be reached in membrane protein analyses at various levels such as elucidation of their primary structure by collision-induced dissociation (CID) and electron-capture dissociation (ECD) mass spectrometry (MS), profiling membrane proteins and their complexes, the discovery of novel protein complexes, definition of their topology, and unambiguous identification of protein-bound ligand(s). This thesis paves the way for better characterization of membrane proteins and their assemblies hinting towards the crucial role(s) they play in maintaining normal cell physiology.

Place, publisher, year, edition, pages
Stockholm: Department of Analytical Chemistry, Stockholm University, 2011. 94 p.
Keyword
Membrane proteins, Proteomics, Escherichia coli, Enterococcus faecalis, Synechocystis, Mass Spectrometry, BN/SDS-PAGE, FT-ICR-MS, Myelin P2 protein
National Category
Analytical Chemistry
Research subject
Analytical Chemistry
Identifiers
urn:nbn:se:su:diva-56848 (URN)978-91-7447-211-0 (ISBN)
Public defence
2011-06-08, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (English)
Opponent
Supervisors
Note
At the time of the doctoral defense, the following paper was unpublished and had a status as follows: Paper 3: Manuscript. Available from: 2011-05-12 Created: 2011-04-28 Last updated: 2012-01-24Bibliographically approved

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