## Abstract The effects on helical stability of weak polar interactions between aromatic side‐chains and the peptide backbone were examined. α‐Helical model peptides, hexa‐Ala, with sequential Tyr replacement, were investigated computationally to obtain the geometries and energetics of the interact
Aromatic interactions in peptides: Impact on structure and function
✍ Scribed by Marcey L. Waters
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2004
- Tongue
- English
- Weight
- 488 KB
- Volume
- 76
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Aromatic interactions, including π–π, cation–π, aryl–sulfur, and carbohydrate–π interactions, have been shown to be prevalent in proteins through protein structure analysis, suggesting that they are important contributors to protein structure. However, the magnitude and significance of aromatic interactions is not defined by such studies. Investigation of aromatic interactions in the context of structured peptides has complemented studies of protein structure and has provided a wealth of information regarding the role of aromatic interactions in protein structure and function. Recent advances in this area are reviewed. © 2004 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2004
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