Dissecting the stability of a beta-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the beta-turn and beta-strand contributions to folding.

Abstract excerpt

NMR studies of the folding and conformational properties of a beta-hairpin peptide, several peptide fragments of the hairpin, and sequence-modified analogues, have enabled the various contributions to beta-hairpin stability in water to be dissected. Temperature and pH-induced unfolding studies indicate that the folding-unfolding equilibrium approximates to a two-state model. The hairpin is highly resistant to...

Topics

• Amino Acid Sequence
• Circular Dichroism
• Computer Simulation
• Hydrogen Bonding
• Hydrogen-Ion Concentration
• Models, Chemical
• Models, Molecular
• Molecular Sequence Data
• Mutation
• Nuclear Magnetic Resonance, Biomolecular
• Peptides
• Protein Denaturation
• Protein Folding