Pressure-induced changes in the fluorescence behavior of red fluorescent proteins.

Pressure-induced changes in the fluorescence behavior of red fluorescent proteins.
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压力诱导的红色荧光蛋白荧光行为变化。

DOI:
10.1021/jp306093h
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发表时间:
2012-08-30
影响因子:
3.3
通讯作者:
Weber, J. Mathias
Weber, J. Mathias
中科院分区:
化学3区
文献类型:
--
作者:
Pozzi, Eric A.;Schwall, Linda R.;Jimenez, Ralph;Weber, J. Mathias

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我们对红色荧光蛋白 TagRFP-S、TagRFP-T、mCherry、mOrange2、mStrawberry 和 mKO 的荧光行为作为高达几 GPa 的压力函数进行了实验研究。 TagRFP-S、TagRFP-T、mOrange2 和 mStrawberry 在施加高于环境条件的压力后,荧光强度最初增加。在较高的压力下,所有正在研究的蛋白质的荧光强度都会急剧下降,这可能是由于蛋白质的变性。在所有研究的蛋白质中,随着压力的增加,荧光光谱出现了小幅蓝移,这表明发色团环境的刚性增加。此外,mOrange2 和 mStrawberry 在一定压力下其荧光光谱表现出强烈且突然的变化。这些变化可能是由于发色团氢键环境的结构改变所致。具有相同或非常相似的发色团的蛋白质之间的行为之间的巨大差异凸显了发色团环境如何影响压力诱导的荧光性能行为。
We present an experimental study on the fluorescence behavior of the red fluorescent proteins TagRFP-S, TagRFP-T, mCherry, mOrange2, mStrawberry, and mKO as a function of pressure up to several GPa. TagRFP-S, TagRFP-T, mOrange2, and mStrawberry show an initial increase in fluorescence intensity upon application of pressure above ambient conditions. At higher pressures, the fluorescence intensity decreases dramatically for all proteins under study, probably due to denaturing of the proteins. Small blue shifts in the fluorescence spectra with increasing pressure were seen in all proteins under study, hinting at increased rigidity of the chromophore environment. In addition, mOrange2 and mStrawberry exhibit strong and abrupt changes in their fluorescence spectra at certain pressures. These changes are likely due to structural modifications of the hydrogen bonding environment of the chromophore. The strong differences in behavior between proteins with identical or very similar chromophores highlight how the chromophore environment contributes to pressure-induced behavior of the fluorescence performance.
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