Effects of Alternative Side Chain Pairings and Reverse Turn Sequences on Antiparallel Sheet Structure in β-Peptide Hairpins
- 24 February 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Organic Letters
- Vol. 6 (6) , 937-940
- https://doi.org/10.1021/ol0364430
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Preparation of Protected syn-α,β-Dialkyl β-Amino Acids That Contain Polar Side Chain FunctionalityThe Journal of Organic Chemistry, 2003
- Parallel Sheet Secondary Structure in β‐PeptidesAngewandte Chemie International Edition in English, 2003
- Asymmetric Synthesis of a New Helix-Forming β-Amino Acid: trans-4-Aminopiperidine-3-carboxylic AcidEuropean Journal of Organic Chemistry, 2003
- β-Peptides: From Structure to FunctionChemical Reviews, 2001
- Τhe β-Peptide Hairpin in Solution: Conformational Study of a β-Hexapeptide in Methanol by NMR Spectroscopy and MD SimulationJournal of the American Chemical Society, 2001
- Stereochemical Control of Hairpin Formation in β-Peptides Containing Dinipecotic Acid Reverse Turn SegmentsJournal of the American Chemical Society, 2000
- Pleated Sheets and Turns ofβ-Peptides with Proteinogenic Side ChainsAngewandte Chemie International Edition in English, 1999
- A β-Peptide Reverse Turn that Promotes Hairpin FormationJournal of the American Chemical Society, 1998
- Antiparallel Sheet Formation in β-Peptide Foldamers: Effects of β-Amino Acid Substitution on Conformational Preference1Journal of the American Chemical Society, 1997
- Nuclear magnetic resonance studies of amidesChemical Reviews, 1970