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...

Full description

Saved in:
Bibliographic Details
Published inOrganic letters Vol. 2; no. 17; pp. 2607 - 2610
Main Authors Huck, Bayard R, Fisk, John D, Gellman, Samuel H
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 24.08.2000
Subjects
Magnetic Resonance Spectroscopy
Nipecotic Acids - chemistry
Peptides - chemical synthesis
Peptides - chemistry
Proline - analogs & derivatives
Protein Structure, Secondary
Spectroscopy, Fourier Transform Infrared
Online AccessGet full text

Cover

More Information
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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1523-7060
1523-7052
DOI:10.1021/ol006120t