ESTIMATION OF THE POLARITY OF THE PROTEIN INTERIOR BY OPTICAL SPECTROSCOPY
ESTIMATION OF THE POLARITY OF THE PROTEIN INTERIOR BY OPTICAL SPECTROSCOPY
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DOI：
10.1038/319070a0
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发表时间：
1986-01-02
期刊：
影响因子：
64.8
通讯作者：
WEBER, G
中科院分区：
文献类型：
--
作者：
MACGREGOR, RB;WEBER, G
肌红蛋白的晶体学研究表明，血红素袋内衬非极性氨基酸残基1。为了估计蛋白质内部的真实极性，某些研究使用了结合荧光团2 -7，其光谱特性反映了其环境的极性。这些研究最常使用1-氨基-8-萘磺酸盐（ANS）作为探针，但原则上更合适的探针是6-丙酰基2-（N，N-二甲基）氨基萘（PRODAN）8。我们合成了一种具有PRODAN的有利光谱特性但对脱肌球蛋白具有更高亲和力的分子：2′-（N，N-二甲基）氨基-6-萘甲酰基-4-反式-环己酸（DANCA），并在此报告其用于确定肌红蛋白血红素口袋的极性。我们的研究结果表明，口袋实际上是一个极性的环境，和极性可以占肽酰胺偶极子。
Crystallographic studies of myoglobin have shown that the haem pocket is lined with nonpolar amino-acid residues1. In order to estimate the true polarity of the interior of proteins, certain studies have used bound fluorophores2–7, the spectroscopic properties of which reflect the polarity of their environment. These studies have most often used l-amino-8-naphthalene sulphonate (ANS) as a probe, but a more suitable probe, in principle, is 6-propionyl 2-(N,N-dimethyl)aminonaphthalene (PRODAN)8. We have synthesized a molecule with the advantageous spectroscopic properties of PRODAN but with a higher affinity for apomyo-globlin: 2′-(N,N-dimenthyl)amino-6-naphthopyl-4-trans-cyclo-hexanoic acid (DANCA), and report here its use to determine the polarity of the myoglobin haem pocket. Our results show that the pocket is actually a polar environment, and the polarity can be accounted for by peptide amide dipoles.