✦ LIBER ✦

Secondary Structure and Membrane Interaction of PR-39, a Pro+Arg-rich Antibacterial Peptide

✍ Scribed by Véronique Cabiaux; Birgitta Agerberths; Jan Johansson; Fabrice Homblé; Erik Goormaghtigh; Jean-Marie Ruysschaert

Book ID: 115130574
Publisher: John Wiley and Sons
Year: 1994
Tongue: English
Weight: 960 KB
Volume: 224
Category: Article
ISSN: 1432-1327
DOI: 10.1111/j.1432-1033.1994.01019.x

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Secondary structure, phospholipid membra

Secondary structure, phospholipid membrane interactions, and fusion activity of two glutamate-rich analogs of influenza hemagglutinin fusion peptide

✍ Eric Assen B. Kantchev; Shu-Fang Cheng; Cheng-Wei Wu; Hung-Jen Huang; Ding-Kwo C 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 350 KB

The effect of Zn2+ on the secondary stru

The effect of Zn2+ on the secondary structure of a histidine-rich fusogenic peptide and its interaction with lipid membranes

✍ H. Binder; K. Arnold; A.S. Ulrich; O. Zschörnig 📂 Article 📅 2000 🏛 Elsevier Science 🌐 English ⚖ 427 KB

Influence of N-terminus modifications on

Influence of N-terminus modifications on the biological activity, membrane interaction, and secondary structure of the antimicrobial peptide hylin-a1

✍ Edson Crusca Jr.; Adrielle A. Rezende; Reinaldo Marchetto; Maria J. S. Mendes-Gi 📂 Article 📅 2011 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 320 KB 👁 2 views

## Abstract Recently the peptide Hy‐a1 (IFGAILPLALGALKNLIK), with antimicrobial activity, was isolated from the skin secretion of the frog Hypsiboas albopunctatus. The aim of the present work was to evaluate four analogues with introduction of acetyl group, Asp or Lys at the N‐terminus of antimicro