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Comparison of the binding of α-helical and β-sheet peptides to a hydrophobic surface

✍ Scribed by STEER, DAVID L. ;THOMPSON, PHILIP E. ;BLONDELLE, SYLVIE E. ;HOUGHTEN, RICHARD A. ;AGUILAR, MARIE-ISABEL

Book ID
110893665
Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
879 KB
Volume
51
Category
Article
ISSN
1397-002X

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Surface active properties of amphiphilic
Surface active properties of amphiphilic sequential isopeptides: Comparison between α-helical and β-sheet conformations
✍ Régine Maget-Dana; Dominique Lelièvre; André Brack 📂 Article 📅 1999 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 155 KB

Poly(Leu-Lys-Lys-Leu) and poly(Leu-Lys) are sequential amphiphilic peptide isomers that adopt respectively an ␣-helical conformation and a ␤-sheet structure in saline solutions and at the air/water interface. The surface active properties of LKKL and LK sequential isopeptides containing 16, 20, and