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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Copper(II) complexation by fragment of central part of FBP28 protein from Mus musculus
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Copper(II) complexation by fragment of central part of FBP28 protein from Mus musculus

机译:铜(II)由亩肌肉的FBP28蛋白的中枢部分片段络合

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摘要

Steady-state and time-resolved fluorescence spectroscopy, UV spectrophotometry and isothermal titration calorimetry techniques were used to study the coordinating properties of the 17aa peptide fragment (D17) derived from the central part of the mouse formin binding protein (FBP28 with the PDB code:1E0L) towards Cu2+ions. All the measurements were run in the 2-(N-morpholino)ethanesulfonic acid buffer (20?mM, pH?6.0). Under experimental conditions the formation of the 1:1 complex of Cu2+ions with D17 is an entropy-driven process. Cu2+ions cause the static fluorescence quenching of the peptide studied through the formation of a non-fluorescent complex. Furthermore, the thermal stability of D17 was discussed based on the results obtained from differential scanning fluorimetry (nanoDSF) data.
机译:使用稳态和时间分辨荧光光谱,UV分光光度法和等温滴定热量法研究,用于研究衍生自小鼠甲蛋白结合蛋白的中心部分(FBP28与PDB代码的17AA肽片段(D17)的配位性质(FBP28: 1E0L)朝向Cu2 +离子。 所有测量都在2-(N-吗啉代)乙磺酸缓冲液(20μm,pH≤6.0)中。 在实验条件下,用D17的Cu 2 +离子的1:1复合物的形成是熵驱动的方法。 Cu2 +离子引起通过形成非荧光复合物研究的肽的静态荧光猝灭。 此外,基于从差示扫描荧光法(NANODSF)数据获得的结果讨论了D17的热稳定性。

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