Secondary structure of an antibacterial peptide Abp3 studied by two-dimensional proton-NMR

Weidong Xia, Qin Liu, Jihui Wu, Youlin Xia, Yunyu Shi, Xianming Qu

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4 Scopus citations

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 languageEnglish (US)
Pages (from-to)299-305
Number of pages7
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1384
Issue number2
DOIs
StatePublished - May 19 1998

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

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