beta-depsipeptides-the effect of a missing and a weakened hydrogen bond on the stability of the beta-peptidic 3(14)-helix

The importance of hydrogen bonding in beta-peptide 3(14)-helices is demonstrated by an NMR analysis of three beta-heptadepsipeptides containing a 3-hydroxybutanoic residue in position 2, 4 or 6.

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Bibliographic Details
Published inChemical communications (Cambridge, England) no. 15; pp. 1598 - 1599
Main Authors Seebach, D, Mahajan, YR, Senthilkumar, R, Rueping, M, Jaun, B
Format Journal Article
LanguageEnglish
Published CAMBRIDGE Royal Soc Chemistry 07.08.2002
Subjects
Chemistry
Chemistry, Multidisciplinary
Circular Dichroism
Hydrogen Bonding
Magnetic Resonance Spectroscopy
Molecular Conformation
Oligopeptides - chemical synthesis
Oligopeptides - chemistry
Oxygen - chemistry
Physical Sciences
Protein Conformation
Science & Technology
SIDE-CHAINS
HELICAL SECONDARY STRUCTURE
NMR
ACID
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Summary:The importance of hydrogen bonding in beta-peptide 3(14)-helices is demonstrated by an NMR analysis of three beta-heptadepsipeptides containing a 3-hydroxybutanoic residue in position 2, 4 or 6.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1359-7345
1364-548X
DOI:10.1039/b204187c