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  Conformational Shift of a β-Hairpin Peptide upon Complex Formation with an Oligo–proline Peptide Studied by Mass Spectrometry

Kölbel, K., Warnke, S., Seo, J., Helden, G. v., Moretti, R., Meiler, J., et al. (2016). Conformational Shift of a β-Hairpin Peptide upon Complex Formation with an Oligo–proline Peptide Studied by Mass Spectrometry. ChemistrySelect, 1(13), 3651-3656. doi:10.1002/slct.201600934.

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 Creators:
Kölbel, Knut1, 2, Author
Warnke, Stephan3, Author              
Seo, Jongcheol3, Author              
Helden, Gert von3, Author              
Moretti, Rocco4, Author
Meiler, Jens4, Author
Pagel, Kevin3, 5, Author              
Sinz, Andrea1, Author
Affiliations:
1Department of Pharmaceutical Chemistry and Bioanalytics, Institute for Pharmacy, Martin-Luther-Universität Halle-Wittenberg, W.-Langenbeck- Straße 4, 06120 Halle (Germany), ou_persistent22              
2Chemistry Department, Universiteit Antwerpen, Campus Groenenborger, Groenenborgerlaan 171 G.V. 416, 2020 Antwerpen (België), ou_persistent22              
3Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              
4Department of Chemistry and the Center for Structural Biology, Vanderbilt University, 465 21st Ave South, BIOSCi/MRBIII, Nashville, TN (USA), ou_persistent22              
5Freie Universität Berlin, Institute of Chemistry and Biochemistry, Takustraße 3, 14195 Berlin (Germany), ou_persistent22              

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 Abstract: So-called super-secondary structures such as the β-hairpin, studied here, form an intermediate hierarchy between secondary and tertiary structures of proteins. Their sequence-derived´pure’ peptide backbone conformation is combined with´remote’ interstrand or interresidue contacts reminiscent of the 3D-structure of full-length proteins. This renders them ideally suited for studying potential nucleation sites of protein folding reactions as well as intermolecular interactions. But β-hairpins do not merely serve as model systems; their unique structure characteristics warrant a central role in structural studies on their own. In this study we applied photo cross-linking in combination with high-resolution mass spectrometry and computational modeling as well as with ion mobility-mass spectrometry to elucidate these structural properties. Using variants of a known β-hairpin representative, the so-called trpzip peptide and its ligands, we found evidence for a conformational transition of the β-hairpin and its impact on ligand binding.

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 Dates: 2016-07-192016-07-222016-08-19
 Publication Status: Published online
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/slct.201600934
 Degree: -

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Title: ChemistrySelect
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: 6 Volume / Issue: 1 (13) Sequence Number: - Start / End Page: 3651 - 3656 Identifier: Other: 2365-6549
CoNE: https://pure.mpg.de/cone/journals/resource/2365-6549