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  Conformation and Dynamics of a Cyclic Disulfide-Bridged Peptide: Effects of Temperature and Solvent

Li, F., Bravo-Rodriguez, K., Phillips, C., Seidel, R. W., Wieberneit, F., Stoll, R., et al. (2013). Conformation and Dynamics of a Cyclic Disulfide-Bridged Peptide: Effects of Temperature and Solvent. The Journal of Physical Chemistry B, 117(13), 3560-3570. doi:10.1021/jp4007334.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-A2D0-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-BE6E-1
Genre: Journal Article

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jp4007334_si_003.pdf (Supplementary material), 3MB
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 Creators:
Li, Fee1, Author
Bravo-Rodriguez, Kenny2, Author              
Phillips, Charlotte3, Author
Seidel, Rüdiger W.4, Author
Wieberneit, Florian5, Author
Stoll, Raphael5, Author
Doltsinis, Nikos L.3, 6, Author
Sánchez-García, Elsa2, Author              
Sander, Wolfram1, Author
Affiliations:
1Lehrstuhl für Organische Chemie II, Ruhr-Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany, escidoc:persistent22              
2Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, DE, escidoc:1950289              
3Department of Physics, King’s College London, WC2R 2LS, London, United Kingdom, escidoc:persistent22              
4Lehrstuhl für Analytische Chemie, Ruhr-Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany, escidoc:persistent22              
5Biomolecular NMR, Ruhr-Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany, escidoc:persistent22              
6Institut für Festkörpertheorie, Universität Münster, Wilhelm-Klemm-Strasse 10, 48149 Münster, Germany, escidoc:persistent22              

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 Abstract: The cyclic disulfide-bridged tetrapeptide cyclo-(Boc-Cys-Pro-Gly-Cys-OMe) (1) was designed as a model for the study of solvent-driven conformational changes in peptides. The three-dimensional structure and dynamics of 1 were studied using a variety of experimental and computational techniques. The crystal structure of 1 reveals a β-turn stabilized by a hydrogen bond between the two cysteine residues. In solution, the UV−CD and NMR analysis of 1 suggest a β-turn II conformation, stable up to 60 °C. The characteristic NMR 13C shifts of the Cβ and Cγ atoms of proline show that the peptide adopts exclusively the energetically favored trans conformation of the peptidyl-prolyl bond. The combination of IR spectroscopy with Car−Parrinello MD simulations and DFT calculations allowed us to assign the absorptions in the amide I region to the individual amino acids. The NH group of Gly, which as hydrogen bond donor competes with the NH group of Cys4 for the carbonyl oxygen atom of Cys1 as hydrogen bond acceptor, plays a relevant role for the structure and spectroscopic properties of the peptide. Since Gly is more exposed to the solvent, its hydrogen-bonding capability can be partially blocked by external solvent molecules in solution or by a second peptide molecule in the crystal. Furthermore, the presence of only one molecule of acetonitrile is sufficient to change the preferred conformation of 1, and even in acetonitrile solution the simulations suggest that on average only one solvent molecule strongly interacts with the cyclic core of the peptide.

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Language(s): eng - English
 Dates: 2013-03-052013-01-252013-03-212013-04-04
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1021/jp4007334
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Title: The Journal of Physical Chemistry B
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: 11 Volume / Issue: 117 (13) Sequence Number: - Start / End Page: 3560 - 3570 Identifier: ISSN: 1520-6106
CoNE: http://pubman.mpdl.mpg.de/cone/journals/resource/1000000000293370_1