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Designer hairpins: 12-Residue peptide 1, containing D-proline, folds to form a two-stranded antiparallel β-sheet in aqueous solution, which causes clustering of the side chains of Trp 2, Tyr 4, Phe 11, and Val 13 (highlighted in the drawing). A similar cluster occurs in the folded state of the protein GB1. Thermodynamic analysis suggests that both the hydrophobic effect and intrinsic interstrand attractions contribute to β-hairpin stability.
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Espinosa et al. (2000) studied this question.
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