Was the β-hairpin fished out from a conformationally defined peptide library of close to 140 000 structures really stabilized? Or was the unexpected Ile residue at the hydrogen-bonded position a mistake in the selection procedure? It seems that the answer is yes, it was. The β-branched side chains of Ile and Val (at position 9) are preferred to stabilize the hydrophobic minicore defined by Trp4, Tyr6, and Tyr11in MBH12, a model β-hairpin peptide (see figure).
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Pastor et al. (2005) studied this question.