Reference : Energetics and Structural Characterization of Isomers Using Ion Mobility and Gas-phas...
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Chemistry
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/179705
Energetics and Structural Characterization of Isomers Using Ion Mobility and Gas-phase H/D Exchange: Learning from Lasso Peptides
English
Hanozin, Emeline mailto [Université de Liège - ULiège > Département de chimie (sciences) > Laboratoire de spectrométrie de masse (L.S.M.), GIGA-R > >]
Morsa, Denis mailto [Université de Liège - ULiège > > Center for Analytical Research and Technology (CART) > >]
De Pauw, Edwin mailto [Université de Liège - ULiège > Département de chimie (sciences) > Laboratoire de spectrométrie de masse (L.S.M.), GIGA-R > >]
27-Jun-2015
Proteomics
Wiley-VCH Verlag Gmbh
early view
1-12
Yes (verified by ORBi)
International
1615-9853
1615-9861
Weinheim
Germany
[en] Ion mobility ; peptides ; folding ; mass spectrometry ; H/D exchange
[en] State-of-the-art characterization of proteins using mass spectrometry namely relies on fragmentation methods which allows exploring featured dissociative reaction pathways. These pathways are often initiated by a series of potentially informative mass-constant conformational changes that are nonetheless frequently overlooked by lack of adequate investigation techniques. In the present study, we propose a methodology to readily address both structural and energetic aspects of stereoisomerization reactions using ion mobility coupled with mass spectrometry. To this end, a commercial spectrometer was used as a reactor comprising an energy resolved collisional activation step intended at promoting controlled conformational changes and a structural assignment step dedicated to the identification of the generated isomers. This identification relies on ion mobility and other on-line coupled techniques, namely an originally designed gas-phase H/D exchange experiment. We here apply this methodology to characterize the isomerization kinetics of capistruin, a 19-residue long lasso-folded peptide. We expect this approach to bring insights into the physical origin of global dissociation thresholds monitored in tandem mass spectrometry experiments and to set a promising basis for quantitative investigations of the stability of different molecular folds.
Giga-Systems Biology and Chemical Biology ; Centre Interfacultaire d'Analyse des Résidus en Traces - CART
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/179705
10.1002/pmic.201400534
http://onlinelibrary.wiley.com/doi/10.1002/pmic.201400534/abstract
This is the peer reviewed version of the following article: Energetics and Structural Characterization of Isomers Using Ion Mobility and Gas-phase H/D Exchange: Learning from Lasso Peptides, which has been published in final form at [10.1002/pmic.201400534]. This article may be used for non-commercial purposes in accordance With Wiley Terms and Conditions for self-archiving.
FP7 ; 278346 - VENOMICS - High-throughput peptidomics and transcriptomics of animal venoms for discovery of novel therapeutic peptides and innovative drug development

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