Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Relaxation behavior.
Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Relaxation behavior.
复制标题
通过自然丰度碳 13 核磁共振波谱研究溶液中蛋白质的各个碳位点。
DOI：
10.1016/s0021-9258(19)41076-4
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发表时间：
1975
期刊：
影响因子：
--
通讯作者：
A. Allerhand
中科院分区：
文献类型：
--
作者：
Eric Oldfield;Raymond S. Norton;A. Allerhand
天然丰度13 C傅里叶变换NMR光谱（在15.18 MHz，在20毫米样品管）的含水天然蛋白质产生许多狭窄的单碳共振的非质子化的芳族碳。这些共振的分配技术。每种技术应用于以下蛋白质中的一种或多种：来自马心和克鲁斯念珠菌的铁细胞色素c、来自马心的铁细胞色素c和氰基铁细胞色素c、来自鸡蛋白色的溶菌酶、来自马和抹香鲸骨骼肌的氰基铁肌红蛋白以及来自马的一氧化碳肌红蛋白。在我们研究过的所有蛋白质光谱中，次甲基芳香碳都产生宽谱带。蛋白质的非质子化芳族碳的窄共振的研究，有利于通过去除这些宽带的卷积-差分方法，最好从噪声调制的非共振质子去耦条件下记录的光谱。我们提出了一个总结的化学位移范围的各种类型的非质子化的芳香族碳的氨基酸残基和血红素的抗磁性蛋白质，根据我们的研究结果，鸡蛋白色溶菌酶，马心铁细胞色素c，马一氧化碳肌红蛋白，和一氧化碳血红蛋白从不同物种的。
Natural abundance 13C Fourier transform NMR spectra (at 15.18 MHz, in 20-mm sample tubes) of aqueous native proteins yield numerous narrow single carbon resonances of nonprotonated aromatic carbons. Techniques for the assignment of these resonances are presented. Each technique is applied to one or more of the following proteins: ferricytochrome c from horse heart and Candida krusei, ferrocytochrome c and cyanoferricytochrome c from horse heart, lysozyme from hen egg white, cyanoferrimyoglobins from horse and sperm whale skeletal muscle, and carbon monoxide myoglobin from horse. In all of the protein spectra we have examined, methine aromatic carbons give rise to broad bands. Studies of the narrow resonances of nonprotonated aromatic carbons of proteins are facilitated by removal of these broad bands by means of the convolution-difference method, preferably from spectra recorded under conditions of noise-modulated off-resonance proton decoupling. We present a summary of the chemical shift ranges for the various types of nonprotonated aromatic carbons of amino acid residues and hemes of diamagnetic proteins, based on our results for hen egg white lysozyme, horse heart ferrocytochrome c, horse carbon monoxide myoglobin, and carbon monoxide hemoglobins from various species...