来自紫色asFP595荧光蛋白和黄色zFP538荧光蛋白发色团的pKa值的构象依赖性。
Conformation dependence of pKa's of the chromophores from the purple asFP595 and yellow zFP538 fluorescent proteins.
作者信息
Nemukhin A V, Topol I A, Grigorenko B L, Savitsky A P, Collins J R
机构信息
Department of Chemistry, M.V. Lomonosov Moscow State University, Leninskie Gory, 1/3, Moscow, 119991, Russian Federation.
出版信息
Theochem. 2008 Aug 30;863(1-3):39-43. doi: 10.1016/j.theochem.2008.05.014.
Two members of the green fluorescent protein family, the purple asFP595 and yellow zFP538 proteins, are perspective fluorescent markers for use in multicolor imaging and resonance energy-transfer applications. We report the results of quantum based calculations of the solution pKa values for selected protonation sites of the denatured asFP595 and zFP538 chromophores in the trans- and cis-conformations in order to add in the interpretation of photophysical properties of these proteins. The pKa values were determined from the theromodynamic cycle based on B3LYP/6-311++G(2df,2p) calculations of the gas phase free energies of the molecules and the B3LYP/6-311++G(d,p) calculations of solvation energies. The results show that the pKa's of the protonation sites of the chromophore from asFP595 noticeably depend on the isomer conformation (cis- or trans-), while those of zFP538 are much less sensitive to isomerization.
绿色荧光蛋白家族的两个成员，紫色的asFP595和黄色的zFP538蛋白，是用于多色成像和共振能量转移应用的有前景的荧光标记物。我们报告了基于量子计算得出的变性asFP595和zFP538发色团在反式和顺式构象中选定质子化位点的溶液pKa值的结果，以便辅助解释这些蛋白质的光物理性质。pKa值是根据热力学循环确定的，该循环基于分子气相自由能的B3LYP/6 - 311++G(2df,2p)计算以及溶剂化能的B3LYP/6 - 311++G(d,p)计算。结果表明，asFP595发色团质子化位点的pKa值明显取决于异构体构象（顺式或反式），而zFP538的pKa值对异构化的敏感性要低得多。
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