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Issue 7, 2005
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Advanced approaches for the characterization of a de novo designed antiparallel coiled coil peptide

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Abstract

We report here an advanced approach for the characterization of the folding pattern of a de novo designed antiparallel coiled coil peptide by high-resolution methods. Incorporation of two fluorescence labels at the C- and N-terminus of the peptide chain as well as modification of two hydrophobic core positions by Phe/[15N,13C]Leu enable the study of the folding characteristics and of distinct amino acid side chain interactions by fluorescence resonance energy transfer (FRET) and NMR spectroscopy. Results of both experiments reveal the antiparallel alignment of the helices and thus prove the design concept. This finding is also supported by molecular dynamics simulations. Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR-MS) in combination with NMR experiments was used for verification of the oligomerization equilibria of the coiled coil peptide.

Graphical abstract: Advanced approaches for the characterization of a de novo designed antiparallel coiled coil peptide

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Publication details

The article was received on 02 Dec 2004, accepted on 07 Feb 2005 and first published on 24 Feb 2005


Article type: Paper
DOI: 10.1039/B418167K
Citation: Org. Biomol. Chem., 2005,3, 1189-1194
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    Advanced approaches for the characterization of a de novo designed antiparallel coiled coil peptide

    K. Pagel, K. Seeger, B. Seiwert, A. Villa, A. E. Mark, S. Berger and B. Koksch, Org. Biomol. Chem., 2005, 3, 1189
    DOI: 10.1039/B418167K

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