de.mpg.escidoc.pubman.appbase.FacesBean
Deutsch
 
Hilfe Wegweiser Impressum Kontakt Einloggen
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  From Compact to String—The Role of Secondary and Tertiary Structure in Charge-Induced Unzipping of Gas-Phase Proteins

Warnke, S., Hoffmann, W., Seo, J., Genst, E. D., Helden, G. v., & Pagel, K. (2017). From Compact to String—The Role of Secondary and Tertiary Structure in Charge-Induced Unzipping of Gas-Phase Proteins. Journal of the American Society for Mass Spectrometry, 28(4), 638-646. doi:10.1007/s13361-016-1551-5.

Item is

Basisdaten

einblenden: ausblenden:
Datensatz-Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-2B94-0 Versions-Permalink: http://hdl.handle.net/21.11116/0000-0000-02E4-C
Genre: Zeitschriftenartikel

Dateien

einblenden: Dateien
ausblenden: Dateien
:
ASMS-D-16-00203R1_manuscript.pdf (beliebiger Volltext), 556KB
Beschreibung:
-
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
2017
Copyright Info:
Springer
Lizenz:
-

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Warnke, Stephan1, Autor              
Hoffmann, Waldemar2, Autor
Seo, Jongcheol1, Autor              
Genst, Erwin De3, Autor
Helden, Gert von1, Autor              
Pagel, Kevin1, 2, Autor              
Affiliations:
1Molecular Physics, Fritz Haber Institute, Max Planck Society, escidoc:634545              
2Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany, escidoc:persistent22              
3Department of ChemistryUniversity of Cambridge, Department of ChemistryUniversity of Cambridge, escidoc:persistent22              

Inhalt

einblenden:
ausblenden:
Schlagwörter: Ion mobility-mass spectrometry; IRMPD spectroscopy; Gas-phase proteins; Secondary structure
 Zusammenfassung: In the gas phase, protein ions can adopt a broad range of structures, which have been investigated extensively in the past using ion mobility-mass spectrometry (IM-MS)-based methods. Compact ions with low number of charges undergo a Coulomb-driven transition to partially folded species when the charge increases, and finally form extended structures with presumably little or no defined structure when the charge state is high. However, with respect to the secondary structure, IM-MS methods are essentially blind. Infrared (IR) spectroscopy, on the other hand, is sensitive to such structural details and there is increasing evidence that helices as well as β-sheet-like structures can exist in the gas phase, especially for ions in low charge states. Very recently, we showed that also the fully extended form of highly charged protein ions can adopt a distinct type of secondary structure that features a characteristic C5-type hydrogen bond pattern. Here we use a combination of IM-MS and IR spectroscopy to further investigate the influence of the initial, native conformation on the formation of these structures. Our results indicate that when intramolecular Coulomb-repulsion is large enough to overcome the stabilization energies of the genuine secondary structure, all proteins, regardless of their sequence or native conformation, form C5-type hydrogen bond structures. Furthermore, our results suggest that in highly charged proteins the positioning of charges along the sequence is only marginally influenced by the basicity of individual residues.

Details

einblenden:
ausblenden:
Sprache(n): eng - Englisch
 Datum: 2016-12-052017-04
 Publikationsstatus: Im Druck publiziert
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1007/s13361-016-1551-5
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Journal of the American Society for Mass Spectrometry
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: New York, NY : Springer
Seiten: - Band / Heft: 28 (4) Artikelnummer: - Start- / Endseite: 638 - 646 Identifikator: ISSN: 1044-0305
CoNE: http://pubman.mpdl.mpg.de/cone/journals/resource/954925590403