English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  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.

Item is

Files

show Files
hide Files
:
c4cp05541a.pdf (Publisher version), 4MB
Name:
c4cp05541a.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
2015
Copyright Info:
RSC
:
2095454.pdf (Copyright transfer agreement), 187KB
 
File Permalink:
-
Name:
2095454.pdf
Description:
-
OA-Status:
Visibility:
Private
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Schubert, Franziska1, Author           
Rossi, Mariana1, 2, Author           
Baldauf, Carsten1, Author           
Pagel, Kevin3, 4, Author           
Warnke, Stephan3, Author           
Helden, Gert von3, Author           
Filsinger, Frank3, Author           
Kupser, Peter3, Author           
Meijer, Gerard3, 5, Author           
Salwiczek, Mario4, Author
Koksch, Beate4, Author
Scheffler, Matthias1, Author           
Blum, Volker1, 6, Author           
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              

Content

show
hide
Free keywords: -
 Abstract: 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.

Details

show
hide
Language(s): eng - English
 Dates: 2014-11-282015-02-112015-02-122015-03-21
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C4CP05541A
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Cambridge, England : Royal Society of Chemistry
Pages: - Volume / Issue: 17 (11) Sequence Number: - Start / End Page: 7373 - 7385 Identifier: ISSN: 1463-9076
CoNE: https://pure.mpg.de/cone/journals/resource/954925272413_1