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

MPG-Autoren
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Warnke,  Stephan
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Seo,  Jongcheol
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Helden,  Gert von
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Pagel,  Kevin
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Freie Universität Berlin, Institute of Chemistry and Biochemistry;

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Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-002B-45B4-C
Zusammenfassung
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.