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Design and synthesis of an α-helical peptide containing periodic proline residues

✍ Scribed by Eiichi Kitakuni; Tokio Horiuchi; Yasushi Oda; Motohisa Oobatake; Haruki Nakamura; Toshiki Tanaka

Book ID
115925764
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
412 KB
Volume
298
Category
Article
ISSN
0014-5793

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Thermodynamic characterization of an art
Thermodynamic characterization of an artificially designed amphiphilic α-helical peptide containing periodic prolines: Observations of high thermal stability and cold denaturation
✍ Eiichi Kitakuni; Yutaka Kuroda; Motohisa Oobatake; Toshiki Tanaka; Haruki Nakamu 📂 Article 📅 2008 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 640 KB

## Abstract To investigate the structural stability of proteins, we analyzed the thermodynamics of an artificially designed 30‐residue peptide. The designed peptide, NH~2~‐EELLPLAEALAPLLEALLPLAEALAPLLKK‐COOH (PERI COIL‐l), with prolines at __i__ + 7 positions, forms a pentameric α‐helical structure

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Twelve- and sixteen-residue peptides have been designed to form tetrameric alpha-helical bundles. Both peptides are capable of folding into amphiphilic alpha-helices, with leucyl residues along one face and glutamyl and lysyl residues along the opposite face. Four such amphiphilic alpha-helices are