title: Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study.
abstract: Can the structures of small to medium-sized proteins be conserved after transfer from the solution phase to the gas phase? A large number of studies have been devoted to this topic, however the answer has not been unambiguously determined to date. A clarification of this problem is important since it would allow very sensitive native mass spectrometry techniques to be used to address problems relevant to structural biology. A combination of ion-mobility mass spectrometry with infrared spectroscopy was used to investigate the secondary and tertiary structure of proteins carefully transferred from solution to the gas phase. The two proteins investigated are myoglobin and β-lactoglobulin, which are prototypical examples of helical and β-sheet proteins, respectively. The results show that for low charge states under gentle conditions, aspects of the native secondary and tertiary structure can be conserved.
authors.affiliation: Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.
authors.forename: Jongcheol
authors.identifier: 0000-0001-5844-4585
authors.initials: J
authors.lastname: Seo
authors.affiliation: Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.
authors.forename: Waldemar
authors.identifier: 0000-0001-6757-3151
authors.initials: W
authors.lastname: Hoffmann
authors.affiliation: Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.
authors.forename: Stephan
authors.identifier: 0000-0001-7481-286X
authors.initials: S
authors.lastname: Warnke
authors.affiliation: Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.
authors.forename: Michael T
authors.initials: MT
authors.lastname: Bowers
authors.affiliation: Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.|Institut für Chemie und Biochemie der, Freien Universität Berlin, Takustrasse 3, 14195, Berlin, Germany.
authors.forename: Kevin
authors.identifier: 0000-0001-8054-4718
authors.initials: K
authors.lastname: Pagel
authors.affiliation: Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany. helden@fhi-berlin.mpg.de.
authors.forename: Gert
authors.identifier: 0000-0001-7611-8740
authors.initials: G
authors.lastname: von Helden
mesh_terms: D007782:Lactoglobulins / Q000737:chemistry*; D013058:Mass Spectrometry; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry*; D011487:Protein Conformation; D012997:Solvents / Q000737:chemistry
chemical_list: D007782:Lactoglobulins; D009211:Myoglobin; D012997:Solvents
keywords: IR spectroscopy; gas-phase reactions; mass spectrometry; protein folding; protein structures