Drift time mass spectrometric protein hydration experiments |
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| Affiliation: | 1. Physical Chemistry I, Otto-Hahn-Str. 6, 44227 Dortmund, Germany;1. ENEA, Dip. Tecnologie Energetiche, C.R. Casaccia, Via Anguillarese 301, 00123, S. Maria di Galeria, Rome, Italy;2. ENEA, Dip. Fusione e Tecnologie per la Sicurezza Nucleare, C.R. Frascati, Via E. Fermi 45, 00044, Frascati RM, Italy;1. Key Laboratory of Macromolecular Science of Shaanxi Province, School of Chemistry & Chemical Engineering, Shaanxi Normal University, Xi''an 710062, PR China;2. School of Chemical and Biomedical Engineering, Nanyang Technological University, Singapore 637459, Singapore |
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| Abstract: | Recent developments in electrospray ionization opened the field of mass spectrometry for macromolecules like proteins. The combination of ionization, drift time spectrometry, and mass spectrometry combines a large field of experimental techniques. In this new field it becomes possible to understand the interactions of isolated proteins with reaction partners like water. The combination of these techniques allows one to determine structural and thermodynamic properties. The experiments presented here give a first insight into the interaction of isolated protein ions with single solvent molecules. Results are presented for proteins like cytochrome C, bovine pancreatic trypsin inhibitor and lysozyme. MD-simulations on the same proteins and conditions as similar as possible to the experiments reflect the experimental results remarkable well. |
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