Role of an Aliphatic-Aromatic Interaction in the Stabilization of a Model β-Hairpin Peptide

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 o...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2005-10, Vol.6 (10), p.1753-1756
Main Authors: Pastor, M. Teresa, Giménez-Giner, Ana, Pérez-Payá, Enrique
Format: Article
Language:English
Subjects:
Amino Acid Sequence
beta-hairpins
Circular Dichroism
libraries
Magnetic Resonance Spectroscopy
Molecular Sequence Data
peptides
Peptides - chemistry
Protein Folding
Protein Structure, Secondary
solvent effects
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Summary: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).
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200500178