首页> 外文期刊>Inorganica Chimica Acta >COMPETITION BETWEEN THE TERMINAL AMINO AND IMIDAZOLE NITROGEN DONORS FOR COORDINATION TO NI(II) IONS IN OLIGOPEPTIDES
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COMPETITION BETWEEN THE TERMINAL AMINO AND IMIDAZOLE NITROGEN DONORS FOR COORDINATION TO NI(II) IONS IN OLIGOPEPTIDES

机译:端氨基酸和咪唑氮供体之间的竞争,以配位寡肽中的Ni(II)离子

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摘要

Spectroscopic and potentiometric studies on Ni(II) complexes with oligopeptides containing a histidine (His) residue in the fourth position of the peptide sequence have shown that imidazole nitrogen can act as the major binding site for metal ions. As a result, coordination of Ni(II) to an imidazole nitrogen of a His residue leads to more stable species than those obtained for linear peptides containing non-coordinating side chains, such as tetraalanine. [References: 21]
机译:Ni(II)配合物与在肽序列第4位含有组氨酸(His)残基的寡肽的光谱和电位分析表明,咪唑氮可以充当金属离子的主要结合位点。结果,Ni(II)与His残基的咪唑氮的配位导致比从包含非配位侧链的线性肽如四丙氨酸获得的那些更稳定的种类。 [参考:21]

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