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首页> 外文期刊>Dalton transactions: An international journal of inorganic chemistry >The unusual coordination abilities of the peptides with βxaaHisGlyHis sequence. the influence of structural modification of the peptide chain on the copper(ii) binding
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The unusual coordination abilities of the peptides with βxaaHisGlyHis sequence. the influence of structural modification of the peptide chain on the copper(ii) binding

机译:βxaaHisGlyHis序列的肽具有异常的配位能力。肽链结构修饰对铜(ii)结合的影响

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摘要

The coordination abilities of tetrapeptides containing β-amino acids towards Cu(ii) ions are presented. The studied tetrapeptides were: Ac-βAlaHisGlyHis, βAlaHisGlyHis, Ac-βAspHisGlyHis, βAspHisGlyHis, Ac-βAspHisGly-dHis and βAspHisGly-dHis. Thorough potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes and the role of free -αCOO~- side chain group in metal binding. The copper(ii) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, EPR, CD) in strict correlation with potentiometric measurements.
机译:提出了含β-氨基酸的四肽对Cu(ii)离子的配位能力。研究的四肽为:Ac-βAlaHisGlyHis,βAlaHisGlyHis,Ac-βAspHisGlyHis,βAspHisGlyHis,Ac-βAspHisGly-dHis和βAspHisGly-dHis。进行了彻底的电位滴定,以建立所得金属-配体络合物的化学计量,以及游离-αCOO--侧链基团在金属结合中的作用。通过与电位测量严格相关地进行详细的光谱分析(UV-Vis,EPR,CD),研究了配合物的铜(ii)配位模式。

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