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Mass spectrometry methodology FT-MS: two-dimensional and technical analysis strategy Top-Down

Director: Tokarski Caroline
Co-director: Rolando Christian
PhD Student: Bray Fabrice


top-down analysis enables the study of theintact protein, allowing identification, primary structuredetermination and localization of post-translationalmodifications (PTMs) directly at the protein level,without the need for enzymatic digests. this technique can be applied to archaeological samples to observe such protein degradation.

Two-dimensional FT-ICR MS has the potential to provide more information on complex samples than either MS/MS or LC–MS/MS because it reveals the fragmentation patterns of all ion species in a complex sample regardless of their abundance. This can be useful in many domains such as the analysis of food, soil, petroleum, rainwater, seawater, biomolecules such as intact proteins, protein digests, and other samples of biological origin.

Molecular characterization of native and modified starches, chemical changes in location of these modified starches and quantitative analysis of additives in starch-based materials

Directeurs : Dr. A. Sabate (INRA Nantes) and A. Mazzah (MSAP Lille)

PhD Student : Chloé Volant

Part of a program funded by the Institute of Excellence IFMAS (winner of the Institute for the Future Investment Program, involving among others industrial Roquette, Mader and Florimond Deprez), this project is a collaboration between the University of Lille and INRA Nantes, in conjunction with industrial IFMAS the project.
Starch as any vegetable raw material, has a structure that varies according to the botanical origin. To maximize its use, guide plant breeding, it is necessary to characterize as thinly as possible native starch. Moreover, to achieve the purpose properties as bio-based materials, the chemical modification is required.

Development of cyclotronic methods for 2D-FT-ICR

Directeur: G. Bodenhausen (UMR 7203 Paris)
Co-directeur: C. Rolando (MSAP Lille)
Thésard: Bouclon Julien

Ion cyclotron resonance mass spectrometry (FT-ICR MS) provide high resolution and mass accuracy, which allow the identification of ions in complex samples. By ion isolation and fragmentation (MS / MS), we could obtain more structural information, but MS/MS methods need a lot of sample and time, because every ion has to be isolated before the fragmentation. In 1987, Pfändler & al. designed a two dimensional FT-ICR MS experiment, in order to fragment ions without any isolation and to see all precursor and fragments in an unique two dimensional spectrum, as in 2D NMR. Because of limitations in electronics and computers, few studies in this method were performed. Since computer ameliorations and numeric electronic utilisation in moderns FT-ICR, the acquisition of large mass range 2D mass spectra is nowadays possible. The original experiment was performed with CID dissociation (collision induced dissociation) in ICR cell which caused loss of resolution. Gas free methods of fragmentation, such as IRMPD and ECD, allow to obtain high resolution 2D mass spectra. Therefore, there is a real interest in the development of 2D FT-ICR MS to an efficient analysis method. Furthermore, ameliorations in 2D NMR could be transposed to 2D FT-ICR MS.