Minimal model systems for β-sheet secondary structure in proteins
- 1 January 1998
- journal article
- review article
- Published by Elsevier in Current Opinion in Chemical Biology
- Vol. 2 (6) , 717-725
- https://doi.org/10.1016/s1367-5931(98)80109-9
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- NMR Structure of a de Novo Designed, Peptide 33mer with Two Distinct, Compact β-Sheet FoldsBiochemistry, 1997
- Construction and Design of β-SheetsAccounts of Chemical Research, 1997
- Structural and Dynamic Properties of a .beta.-Hairpin-Forming Linear Peptide. 1. Modeling Using Ensemble-Averaged ConstraintsJournal of the American Chemical Society, 1995
- 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
- Structural and Dynamic Properties of a .beta.-Hairpin-Forming Linear Peptide. 2. 13C NMR Relaxation AnalysisJournal of the American Chemical Society, 1995
- A short linear peptide that folds into a native stable β-hairpin in aqueous solutionNature Structural & Molecular Biology, 1994
- Dissecting the Structure of a Partially Folded Protein: Circular Dichroism and Nuclear Magnetic Resonance Studies of Peptides from UbiquitinJournal of Molecular Biology, 1993
- NMR evidence of a short linear peptide that folds into a .beta.-hairpin in aqueous solutionJournal of the American Chemical Society, 1993
- Tendamistat (12–26) fragmentEuropean Journal of Biochemistry, 1991
- β-Hairpin families in globular proteinsNature, 1985