Selective Aromatic Interactions in β-Hairpin Peptides
- 18 July 2002
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 124 (32) , 9372-9373
- https://doi.org/10.1021/ja0262481
Abstract
To probe the selectivity possible in hydrophobic clusters, we have compared the cross-strand interactions of phenylalanine (Phe) and cyclohexylalanine (Cha) in a β-hairpin peptide. We have found a preference for self-association among the aromatic residues, which provides 0.55 kcal/mol in stability relative to Cha-Cha cross-strand pair. NMR analysis of the Phe-Phe cross-strand pair indicates that it interacts in an edge-face interaction, despite the fact that it is highly solvent-exposed. The interaction geometry as well as the enthalpic and entropic values for the peptide containing the Phe-Phe cross-strand pair suggest that the preference for self-association arises from inherent differences in the nature of aromatic and aliphatic interactions in water.Keywords
This publication has 13 references indexed in Scilit:
- Interplay between hydrophobic cluster and loop propensity in β-hairpin formationJournal of Molecular Biology, 2001
- A Minimal Peptide Scaffold for β-Turn Display: Optimizing a Strand Position in Disulfide-Cyclized β-HairpinsJournal of the American Chemical Society, 2000
- Determinants of strand register in antiparallel β‐sheets of proteinsProtein Science, 1998
- Origin of β-Hairpin Stability in Solution: Structural and Thermodynamic Analysis of the Folding of a Model Peptide Supports Hydrophobic Stabilization in WaterJournal of the American Chemical Society, 1998
- De novo design and structural analysis of a model β-hairpin peptide systemNature Structural & Molecular Biology, 1996
- An analysis of side chain interactions and pair correlations within antiparallel β‐sheets: The differences between backbone hydrogen‐bonded and non‐hydrogen‐bonded residue pairsProteins-Structure Function and Bioinformatics, 1995
- Crystal structure of CspA, the major cold shock protein of Escherichia coli.Proceedings of the National Academy of Sciences, 1994
- Molecular Torsion Balance for Weak Molecular Recognition Forces. Effects of "Tilted-T" Edge-to-Face Aromatic Interactions on Conformational Selection and Solid-State StructureJournal of the American Chemical Society, 1994
- NMR evidence of a short linear peptide that folds into a .beta.-hairpin in aqueous solutionJournal of the American Chemical Society, 1993
- Aromatic-Aromatic Interaction: A Mechanism of Protein Structure StabilizationScience, 1985