Promotion of sheet formation in alpha-peptide strands by a beta-peptide reverse turn |
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Authors: | Huck B R Fisk J D Gellman S H |
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Affiliation: | Department of Chemistry and Graduate Program in Biophysics, University of Wisconsin, Madison 53706, USA. |
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Abstract: | [structure: see text]We show that a tetrapeptide with a heterogeneous backbone, i.e., with two different classes of amino acid residues, adopts a hairpin conformation in which each type of residue plays a different structural role. The alpha-residues at the ends form hydrogen bonds characteristic of antiparallel beta-sheet secondary structure, while the central di-beta-peptide segment forms a reverse turn. The configuration of the turn residues is critical to sheet formation. |
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