Promotion of Sheet Formation in α-Peptide Strands by a β-Peptide Reverse Turn

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 α-residues at the ends form hydrogen bonds characteristic of antiparallel β-sheet sec...

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Bibliographic Details
Published in:Organic letters 2000-08, Vol.2 (17), p.2607-2610
Main Authors: Huck, Bayard R, Fisk, John D, Gellman, Samuel H
Format: Article
Language:English
Subjects:
Magnetic Resonance Spectroscopy
Nipecotic Acids - chemistry
Peptides - chemical synthesis
Peptides - chemistry
Proline - analogs & derivatives
Protein Structure, Secondary
Spectroscopy, Fourier Transform Infrared
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Summary: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 α-residues at the ends form hydrogen bonds characteristic of antiparallel β-sheet secondary structure, while the central di-β-peptide segment forms a reverse turn. The configuration of the turn residues is critical to sheet formation.
ISSN:1523-7060
1523-7052
DOI:10.1021/ol006120t