NMR-Solution Structures of Fluoro-Substitutedβ-Peptides: A314-Helix and a Hairpin Turn. The First Case of a 90° OCCF Dihedral Angle in anα-Fluoro-Amide Group-Reference-Cited by-同舟云学术

NMR-Solution Structures of Fluoro-Substitutedβ-Peptides: A314-Helix and a Hairpin Turn. The First Case of a 90° OCCF Dihedral Angle in anα-Fluoro-Amide Group

Published:2007-12 Issue:12 Volume:90 Page:2251-2273
ISSN:0018-019X
Container-title:Helvetica Chimica Acta
language:en
Short-container-title:HCA

Author:

Mathad Raveendra I.,Jaun Bernhard,Flögel Oliver,Gardiner James,Löweneck Markus,Codée Jeroen D. C.,Seeberger Peter H.,Seebach Dieter,Edmonds Michael K.,Graichen Florian H. M.,Abell Andrew D.

Publisher

Wiley

Subject

Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Drug Discovery,Biochemistry,Catalysis

Reference55 articles.

1. The World ofβ- andγ-Peptides Comprised of Homologated Proteinogenic Amino Acids and Other Components

2. Helices and other secondary structures of β- and γ-peptides

3. NMR-Solution Structures in Methanol of anα-Heptapeptide, of aβ3/β2-Nonapeptide, and of an all-β3-Icosapeptide Carrying the 20 Proteinogenic Side Chains

4. The Fourth Helical Secondary Structure of β-Peptides: The (P)-28-Helix of a β-Hexapeptide Consisting of (2R,3S)-3-Amino-2-hydroxy Acid Residues

5. Synthesis and CD Spectra of Fluoro- and Hydroxy-Substituted -Peptides

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