Mechanisms of quenching of Alexa fluorophores by natural amino acids.
Mechanisms of quenching of Alexa fluorophores by natural amino acids.
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DOI：
10.1021/ja100500k
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发表时间：
2010-06-02
影响因子：
15
通讯作者：
Webb, Watt W.
中科院分区：
文献类型：
--
作者：
Chen, Huimin;Ahsan, Syed S.;Santiago-Berrios, Mitk'El B.;Abruna, Hector D.;Webb, Watt W.
荧光团被它们共价标记的相同蛋白质猝灭是一种既不为人所知也不为人所知的现象。通常假设荧光团不受其靶蛋白的干扰。然而，已经观察到，连接的荧光团可以通过与相同蛋白质内的氨基酸接触而猝灭，并且这种性质已经被利用来报告蛋白质的构象状态变化或分子内动力学。我们在这篇文章中表明，Alexa染料的荧光实际上是通过静态和动态猝灭机制的组合与Trp，Tyr，Met和His残基的相互作用而猝灭的。鉴于这一发现，在解释涉及蛋白质荧光强度定量测量的数据时，应考虑分子内猝灭的潜在影响。
Quenching of fluorophores by the same proteins that they covalently label is a phenomenon that is neither well-known nor well-characterized. It is often assumed that fluorophores are unperturbed by their target proteins. However, it has been observed that attached fluorophores can be quenched by contact with amino acids within the same protein, and this property has been exploited to report on changing conformational states or intramolecular dynamics of proteins. We show in this communication that fluorescence of Alexa dyes is, in fact, quenched by interactions with Trp, Tyr, Met, and His residues through a combination of static and dynamic quenching mechanisms. In light of this finding, the potential effect of intramolecular quenching should be considered in the interpretation of data that involves quantitative measurements of fluorescence intensity in proteins.
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影响因子：
3.2
作者：
Panchuk-Voloshina, N;Haugland, RP;Haugland, RP
通讯作者：
Haugland, RP
DOI：
10.1073/pnas.211440398
发表时间：
2001-10-09
影响因子：
11.1
作者：
Zhong, DP;Zewail, AH
通讯作者：
Zewail, AH
影响因子：
2.9
作者：
Götz, M;Hess, S;Michel-Beyerle, ME
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Michel-Beyerle, ME
影响因子：
4.7
作者：
Marmé, N;Knemeyer, JP;Wolfrum, J
通讯作者：
Wolfrum, J
影响因子：
15
作者：
Vaiana, AC;Neuweiler, H;Smith, JC
通讯作者：
Smith, JC