Cover Picture: Structural Insights into the Trp-Cage Folding Intermediate Formation (Chem. Eur. J. 8/2013)

Authors

  • Petra Rovó,

    1. Laboratory of Structural Chemistry and Biology, Institute of Chemistry and Protein Modeling Group of HAS-ELTE, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/A (Hungary)
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  • Pál Stráner,

    1. Laboratory of Structural Chemistry and Biology, Institute of Chemistry and Protein Modeling Group of HAS-ELTE, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/A (Hungary)
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  • Dr. András Láng,

    1. Laboratory of Structural Chemistry and Biology, Institute of Chemistry and Protein Modeling Group of HAS-ELTE, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/A (Hungary)
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  • István Bartha,

    1. Institute of Biology, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/C (Hungary)
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  • Kristóf Huszár,

    1. Institute of Mathematics, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/C (Hungary)
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  • Prof. Dr. László Nyitray,

    1. Department of Biochemistry, Institute of Biology, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/C (Hungary)
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  • Prof. Dr. András Perczel

    Corresponding author
    1. Laboratory of Structural Chemistry and Biology, Institute of Chemistry and Protein Modeling Group of HAS-ELTE, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/A (Hungary)
    • Laboratory of Structural Chemistry and Biology, Institute of Chemistry and Protein Modeling Group of HAS-ELTE, Eötvös Loránd University, 1117 Budapest, Pázmány Péter sétány 1/A (Hungary)
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Abstract

original image

The folding energy landscape of the smallest protein, the 20-residue long Trp-cage, is more rugged than expected. Temperature-dependent NMR measurements revealed that at neutral pH the final step of the Trp-cage folding is a fast secondary structural rearrangement: the short α-helical G11–G15 segment of the intermediate (I) converts into a 310-helix and thus, the polypeptide adopts the most stable, folded (F) structure. At acidic pH the isomerization of the G11[BOND]P12 peptide bond slows down the folding process: two off-pathway intermediate unfolded states (U′ and U′′) emerge. These two states have no native-like structure and show elevated internal mobility. For more information see the Full Paper by A. Perczel et al. on page 2628 ff.

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