An Oligomeric Ser-Pro Dipeptide Mimetic Assuming the Polyproline II Helix Conformation

A hexapeptide assembled from dipeptide building blocks assumes the secondary structure of the polyproline II (PPII) helix. Side chain-to-backbone hydrogen bonds stabilize peptide torsions next to the fused ring systems. The solution structure of the polyhydroxylated peptide was studied by spectrosco...

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Bibliographic Details
Published inJournal of the American Chemical Society Vol. 124; no. 29; pp. 8548 - 8549
Main Authors Tremmel, Peter, Geyer, Armin
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 24.07.2002
Subjects
Biological and medical sciences
Conformational dynamics in molecular biology
Dipeptides - chemistry
Fundamental and applied biological sciences. Psychology
Lactams - chemistry
Molecular biophysics
Molecular Conformation
Molecular Mimicry
Nuclear Magnetic Resonance, Biomolecular
Peptides - chemistry
Protein Conformation
Thiazoles - chemistry
Sulfur nitrogen heterocycle
Molecular structure
Conformational analysis
Bicyclic compound
Proline polymer
NMR spectrometry
Helical structure
Amphiphilic compound
Hexapeptide
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Summary:A hexapeptide assembled from dipeptide building blocks assumes the secondary structure of the polyproline II (PPII) helix. Side chain-to-backbone hydrogen bonds stabilize peptide torsions next to the fused ring systems. The solution structure of the polyhydroxylated peptide was studied by spectroscopic methods.
Bibliography:istex:41835447CFFEC8799CC68C22697AACFC0744B022
ark:/67375/TPS-JCSMXS9T-2
ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0002-7863
1520-5126
DOI:10.1021/ja026098u