Rules for Antiparallel β-Sheet Design: d-Pro-Gly Is Superior to l-Asn-Gly for β-Hairpin Nucleation1
- 22 April 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (17) , 4236-4237
- https://doi.org/10.1021/ja973704q
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- Analysis and prediction of the different types of β-turn in proteinsPublished by Elsevier ,2004
- Stereochemical Requirements for β-Hairpin Formation: Model Studies with Four-Residue Peptides and DepsipeptidesJournal of the American Chemical Society, 1996
- A 2,3‘-Substituted Biphenyl-Based Amino Acid Facilitates the Formation of a Monomeric β-Hairpin-like Structure in Aqueous Solution at Elevated TemperatureJournal of the American Chemical Society, 1996
- A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpinNature Structural & Molecular Biology, 1995
- "Mirror image" reverse turns promote .beta.-hairpin formationJournal of the American Chemical Society, 1994
- Accommodating Sequence Changes in β-Hairpins in ProteinsJournal of Molecular Biology, 1993
- The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopyBiochemistry, 1992
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- β-Hairpin families in globular proteinsNature, 1985
- Beta poly(l-lysine): A model system for biological self-assemblyJournal of Molecular Biology, 1974