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The turn sequence directs beta-strand alignment in designed beta-hairpins
E de Alba1, M Rico, M A Jiménez
1Instituto de Estructura de la Materia, Consejo Superior de Investigaciones Cientificas, Madrid, Spain.
Protein Science : a Publication of the Protein Society
|December 14, 1999
Summary
The turn sequence in designed peptides is crucial for determining beta-hairpin structure, even in longer peptides with more interactions. This confirms the turn
Area of Science:
- Biochemistry
- Structural Biology
- Peptide Chemistry
Background:
- Previous studies indicated beta-turn sequences dominate beta-hairpin formation in short peptides.
- Longer peptides with more interactions require further investigation into factors governing beta-hairpin structure.
Purpose of the Study:
- To design and structurally characterize longer beta-hairpin forming peptides.
- To assess the influence of turn sequences versus cross-strand interactions in longer beta-hairpins.
- To investigate the role of a specific salt bridge in beta-hairpin stability and aggregation.
Main Methods:
- Design and synthesis of three pentadecapeptides based on previous decapeptide models.
- 1H Nuclear Magnetic Resonance (NMR) spectroscopy for conformational analysis.
- Analysis of peptide behavior (monomeric vs. self-associating) and secondary structure.
Main Results:
- Identical strand sequences in the designed pentadecapeptides resulted in different beta-hairpin structures.
- The beta-turn sequence was confirmed as the primary determinant of beta-hairpin type.
- One peptide formed intermolecular salt bridges, suggesting self-association.
Conclusions:
- The beta-turn sequence plays a predominant role in directing beta-hairpin formation in designed peptides, irrespective of length.
- Designed peptides can adopt diverse beta-hairpin structures driven by turn sequence variations.
- Turn sequence control is a key strategy for designing peptides with specific beta-hairpin conformations.