Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques.
Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques.
复制标题
通过相敏二维技术对抹香鲸肌红蛋白一氧化碳复合物的 1H 核磁共振谱进行共振分配。
DOI：
10.1016/0022-2836(87)90378-0
复制
发表时间：
1987
影响因子：
5.6
通讯作者：
Wright,PE
中科院分区：
文献类型：
--
作者：
Dalvit,C;Wright,PE
相敏二维核磁共振实验已经被用于获得抹香鲸肌红蛋白的一氧化碳复合物的广泛的质子共振分配。在分配过程中，多个量子实验尤为重要。这些任务是迄今为止最完整的蛋白质的这种高分子量（约18,000）的报告，并使新的和全面的研究在溶液中的一氧化碳-肌红蛋白的结构和动力学。报告了7个组氨酸残基的分析结果，包括关键的近端和远端组氨酸。其中大多数与文献中已有的任务不一致。现在的N. M.数据表明组氨酸24（B5）和119（GH 1）彼此氢键结合，并且与中子衍射数据相反，表明His 24在pH大于5时不质子化。所有苯丙氨酸和酪氨酸残基的芳环都经历围绕环轴的快速翻转。Leu 89（F4）和Phe 138（H15）的侧链与大的疏水空腔相邻，是特别移动的。
Phase-sensitive two-dimensional nuclear magnetic resonance (n.m.r.) experiments have been used to obtain extensive proton resonance assignments for the carbon monoxide complex of sperm whale myoglobin. Multiple quantum experiments were particularly important in the assignment procedure. The assignments are the most complete yet reported for a protein of such high molecular weight (approximately 18,000) and make possible new and comprehensive studies of the structure and dynamics of carbonmonoxy-myoglobin in solution. Assignments for seven of the histidine residues are reported, including the critical proximal and distal histidines. Most of these are at variance with the assignments already in the literature. The present n.m.r. data indicate that histidines 24 (B5) and 119 (GH1) are hydrogen bonded to each other and, in contrast to neutron diffraction data, show that His24 does not protonate at pH greater than 5. The aromatic rings of all the phenylalanine and tyrosine residues undergo rapid flips about the ring axis. The side-chains of Leu89 (F4) and Phe138 (H15), which border a large hydrophobic cavity, are particularly mobile.