Molecular simulations to determine the chelating mechanisms of various metal ions to the his-tag motif: A preliminary study

Hsuan Liang Liu, Yih Ho, Chia Ming Hsu

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16 Citations (Scopus)


In the present study, molecular simulations were performed to investigate the chelating mechanisms of various metal ions to the His-tag motifs with various His residues. The chelation mostly involved the i and i+2 His residues for Ni2+, Zn2+, Cu2+, and Co2+, while the cooperation of 3 His residues was necessary when Fe3+ was involved in chelation with His-tags having more than 4 His residues. Metal ion was best fitted into the pocket formed by the imidazole nitrogens while it was about equally located among these nitrogen atoms. His-tag6 was found to have little effect on the structural integrity while the target protein contains more than 68 amino acid residues. Ni2+ interacted with the imidazole nitrogen of His3 in the beginning of chelation, and then entered into the pocket formed by His3 and His5 at 4 ns during the 10 ns molecular dynamics simulations. The fast chelating process resulted in successful application of IMAC techniques in efficient protein purification.

Original languageEnglish
Pages (from-to)31-41
Number of pages11
JournalJournal of Biomolecular Structure and Dynamics
Issue number1
Publication statusPublished - Aug 2003



  • Chelating
  • His-tag
  • IMAC
  • Molecular dynamics
  • Molecular simulations

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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