Parallel Sheet Secondary Structure in β‐Peptides
- 28 May 2003
- journal article
- research article
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 42 (21), 2402-2405
- https://doi.org/10.1002/anie.200350932
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- Peptide models of protein β-sheets: design, folding and insights into stabilising weak interactionsJournal of the Chemical Society, Perkin Transactions 2, 2001
- Synthesis and Structural Analysis of a β-Hairpin Peptide Containing a Sugar Amino AcidEuropean Journal of Organic Chemistry, 2001
- An Unnatural Amino Acid that Mimics a Tripeptide β-Strand and Forms β-Sheetlike Hydrogen-Bonded Dimers [J. Am. Chem. Soc. 2000, 122, 7654-7661].Journal of the American Chemical Society, 2001
- Pleated Sheets and Turns ofβ-Peptides with Proteinogenic Side ChainsAngewandte Chemie International Edition, 1999
- A β-Peptide Reverse Turn that Promotes Hairpin FormationJournal of the American Chemical Society, 1998
- Conformational Analysis of Peptides and Pseudopeptides Incorporating an endo-(2S,3R)-Norborn-5-ene Residue as a Turn InducerThe Journal of Organic Chemistry, 1998
- Antiparallel Sheet Formation in β-Peptide Foldamers: Effects of β-Amino Acid Substitution on Conformational Preference1Journal of the American Chemical Society, 1997
- Stereochemical Requirements for β-Hairpin Formation: Model Studies with Four-Residue Peptides and DepsipeptidesJournal of the American Chemical Society, 1996
- A Designed β-Hairpin PeptideBiochemical and Biophysical Research Communications, 1995
- MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopyJournal of Magnetic Resonance (1969), 1985