Abstract
An antibacterial peptide Abp3, an analogue of cecropin B, was investigated by two-dimensional proton-NMR at pH 5.0 in aqueous solution with 15% (v/v) hexafluoroisopropanol. The peptide, which consists of 35 amino acids, was synthesized chemically. Most resonances of the main-chain and side-chain protons were assigned. Several medium range NOE connectivities were observed, showing two separate α-helices with one amphiphilic in N-terminal domain (residues 5-21) and the other hydrophobic in C-terminal domain (residues 25-35) and a hinge region between them. The J coupling constants and the chemical shifts in these sections also supported the conclusion. Copyright (C) 1998 Elsevier Science B.V.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 299-305 |
| Number of pages | 7 |
| Journal | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology |
| Volume | 1384 |
| Issue number | 2 |
| DOIs | |
| State | Published - May 19 1998 |
| Externally published | Yes |
Bibliographical note
Funding Information:The work was supported by Grant No. 8512-II-12 from the National Commission of Science and Technology of China, Grant No. J-6-07 from the Chinese Academy of Science, and Grant No. 863-103-13-03-01 from the Chinese High Technology Project.
Keywords
- Abp3
- Cecropin
- Chemical shift
- NMR
- NOE
- Secondary structure