Evidence for protein conformational change at a Au(110)/protein interface.

Evidence for protein conformational change at a Au(110)/protein interface.
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DOI:
10.1209/0295-5075/83/18004
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发表时间:
2008-07
期刊:
Europhysics letters
影响因子:
--
通讯作者:
Weightman P
Weightman P
中科院分区:
其他
文献类型:
--
作者:
Messiha HL;Smith CI;Scrutton NS;Weightman P

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有证据表明,反射各向异性光谱(RAS)可以提供实时测量的构象变化的蛋白质的电子转移反应引起的。细菌电子转移黄素蛋白(ETF)已被修饰,以便吸附在Au(110)电极上,并使可逆的电子转移到蛋白质辅因子在介质的情况下。在这种蛋白质的RAS中观察到可逆的变化,这些变化被解释为伴随电子转移的构象变化。
Evidence is presented that reflection anisotropy spectroscopy (RAS) can provide real-time measurements of conformational change in proteins induced by electron transfer reactions. A bacterial electron transferring flavoprotein (ETF) has been modified so as to adsorb on an Au(110) electrode and enable reversible electron transfer to the protein cofactor in the absence of mediators. Reversible changes are observed in the RAS of this protein that are interpreted as arising from conformational changes accompanying the transfer of electrons.
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影响因子: 2.9
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