期刊
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
卷 21, 期 1, 页码 31-41出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2003.10506903
关键词
molecular simulations; chelating; His-tag; molecular dynamics; IMAC
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 42 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.
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