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  Exploring the conformational preferences of 20-residue peptides in isolation: Ac-Ala19-Lys + H+ vs. Ac-Lys-Ala19 + H+ and the current reach of DFT

Schubert, F., Rossi, M., Baldauf, C., Pagel, K., Warnke, S., Helden, G. v., et al. (2015). Exploring the conformational preferences of 20-residue peptides in isolation: Ac-Ala19-Lys + H+ vs. Ac-Lys-Ala19 + H+ and the current reach of DFT. Physical Chemistry Chemical Physics, 17(11), 7373-7385. doi:10.1039/C4CP05541A.

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Schubert, Franziska1, Autor           
Rossi, Mariana1, 2, Autor           
Baldauf, Carsten1, Autor           
Pagel, Kevin3, 4, Autor           
Warnke, Stephan3, Autor           
Helden, Gert von3, Autor           
Filsinger, Frank3, Autor           
Kupser, Peter3, Autor           
Meijer, Gerard3, 5, Autor           
Salwiczek, Mario4, Autor
Koksch, Beate4, Autor
Scheffler, Matthias1, Autor           
Blum, Volker1, 6, Autor           
Affiliations:
1Theory, Fritz Haber Institute, Max Planck Society, ou_634547              
2Physical and Theoretical Chemistry Laboratory, University of Oxford, OX13QZ Oxford, UK, ou_persistent22              
3Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              
4Institut für Chemie und Biochemie - Organische Chemie, Freie Universität Berlin, D-14195 Berlin, Germany, ou_persistent22              
5Radboud University Nijmegen, 65000 HC Nijmegen, The Netherlands, ou_persistent22              
6Duke University, MEMS Department, Durham, NC 27708, USA, ou_persistent22              

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 Zusammenfassung: A reliable, quantitative prediction of the structure of peptides based on their amino-acid sequence information is an ongoing challenge. We here explore the energy landscape of two unsolvated 20-residue peptides that result from a shift of the position of one amino acid in otherwise the same sequence. Our main goal is to assess the performance of current state-of-the-art density- functional theory for predicting the structure of such large and complex systems, where weak interactions such as dispersion or hydrogen bonds play a crucial role. For validation of the theoretical results, we employ experimental gas-phase ion mobility-mass spectrometry and IR spectroscopy. While unsolvated Ac-Ala19-Lys + H+ will be shown to be a clear helix seeker, the structure space of Ac-Lys-Ala19 + H+ is more complicated. Our first-principles structure-screening strategy using the dispersion-corrected PBE functional (PBE+vdWTS ) identifies six distinctly different structure types competing in the low-energy regime (≈16 kJ/mol). For these structure types, we analyze the influence of the PBE and the hybrid PBE0 functional coupled with either a pairwise dispersion correction (PBE+vdWTS, PBE0+vdWTS) or a many-body dispersion correction (PBE+MBD∗, PBE0+MBD∗). We also take harmonic vibrational and rotational free energy into account. Including this, the PBE0+MBD∗ functional predicts only one unique conformer to be present at 300 K. We show that this scenario is consistent with both experiments.

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Sprache(n): eng - English
 Datum: 2014-11-282015-02-112015-02-122015-03-21
 Publikationsstatus: Erschienen
 Seiten: 14
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1039/C4CP05541A
 Art des Abschluß: -

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Titel: Physical Chemistry Chemical Physics
  Kurztitel : Phys. Chem. Chem. Phys.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Cambridge, England : Royal Society of Chemistry
Seiten: - Band / Heft: 17 (11) Artikelnummer: - Start- / Endseite: 7373 - 7385 Identifikator: ISSN: 1463-9076
CoNE: https://pure.mpg.de/cone/journals/resource/954925272413_1