Energetics of Weak Interactions in a β-hairpin Peptide: Electrostatic and Hydrophobic Contributions to Stability from Lysine Salt Bridges
- 30 November 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 121 (50) , 11615-11620
- https://doi.org/10.1021/ja992029c
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Strength and co-operativity of contributions of surface salt bridges to protein stabilityPublished by Elsevier ,2006
- Dissecting the stability of a β-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the β-turn and β-strand contributions to folding 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- Co-operative interactions during protein foldingJournal of Molecular Biology, 1992
- The folding of an enzyme: VI. The folding pathway of barnase: Comparison with theoretical modelsJournal of Molecular Biology, 1992
- The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopyBiochemistry, 1992
- Solid model compounds and the thermodynamics of protein unfoldingJournal of Molecular Biology, 1991
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- Aromatic-aromatic interactions and protein stabilityJournal of Molecular Biology, 1991
- Ion-pairs in proteinsJournal of Molecular Biology, 1983
- Receptor-based design of dihydrofolate reductase inhibitors: comparison of crystallographically determined enzyme binding with enzyme affinity in a series of carboxy-substituted trimethoprim analogsJournal of Medicinal Chemistry, 1982