Proton nuclear magnetic resonance study of histidine ionizations in myoglobins of various species. Specific assignment of individual resonances.
Proton nuclear magnetic resonance study of histidine ionizations in myoglobins of various species. Specific assignment of individual resonances.
复制标题
不同物种肌红蛋白中组氨酸电离的质子核磁共振研究。
DOI：
10.1021/bi00617a019
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发表时间：
1978
期刊：
影响因子：
2.9
通讯作者：
F. Gurd
中科院分区：
文献类型：
--
作者：
L. H. Botelho;F. Gurd
Lynne H.Botelho*和Frank R.N.Gurd*摘要：根据在220 MHz观察到的C-2质子共振，对来自16个物种的一系列肌红蛋白的残留物进行了研究和归属，这些物种包括12个鲸目动物、2个鳍足动物、马和人。从抹香鲸、矮抹香鲸、须鲸、小须鲸、座头鲸、加州灰鲸、太平洋普通海豚、领航鲸、亚马逊河海豚、宽吻海豚、普通江豚和大理江豚的肌肉中分离到鲸目动物肌红蛋白。鳍脚类动物是海豹和加州海狮。各种肌红蛋白在其已知序列中含有9至13个组氨酸残基。明显可分辨的、滴定组氨酸Ce质子共振质子核磁共振能够产生关于较小的、特征良好的蛋白质的直接和详细的信息(Meadow等人，1967；Wüthrich等人，1970；Migchelson和Beintema，1973；Cohen和Hayes，1974；Markley，1975)。本篇论文和本期的下一篇论文(Botelho等人，1978)讨论了组氨酸pk值的测定以及一些构象变化，这些变化可以通过观察肌红蛋白中的组氨酸C-2质子共振来识别。用这种方法研究了16种动物的一组肌红蛋白(Botelho，1975)。这些肌红蛋白在同源多肽序列中提供了相当大范围的变异。在这一范围内，对抹香鲸、须鲸、海豚和江豚这三个鲸目动物科进行了重点研究，以提供一些密切的结构比较(Jones等人，1977)。自从核磁共振数据收集和首次分析以来，这些肌红蛋白的大部分序列已经被确定(Botelho，1975)。到目前为止遇到的每一种氨基酸替代都被发现定性地符合抹香鲸铁肌红蛋白的三维结构(Watson，1969；Takano，1977)。在所研究的物种之间，在本工作和相关研究中已经注意到许多光谱和其他物理上的相似之处(Wüthrich等人，1970；Hartzell等人，1968a，b；Marks等人，1971；Friend等人，1977)。因此，这组肌红蛋白物种提供了一组结构上相同的蛋白质，可以使用
Lynne H. Botelho* and Frank R. N. Gurd* abstract: Individual residues in a series of myoglobins from 16 species, comprising 12 cetaceans, 2 pinnipeds, horse, and man, were examined and assigned in terms of C-2 proton resonances observed at 220 MHz. The cetacean myoglobins ex-amined were isolated from muscles of sperm whale, dwarf sperm whale, sei whale, minke whale, humpback whale, Cal-ifornia grey whale, Pacific common dolphin, pilot whale, Amazon River dolphin, bottlenosed dolphin, common or har-bor porpoise, and Dali porpoise. The pinnipeds were harbor seal and California sea lion. The various myoglobins contained between 9 and 13 histidine residues in their known sequences. Clearly resolvable, titrating histidine Ce proton resonancesProton NMR is capable of yielding direct and detailed in-formation about the smaller, well-characterized proteins (Meadows et al., 1967; Wüthrich et al., 1970; Migchelson and Beintema, 1973; Cohen and Hayes, 1974; Markley, 1975). The present paper and the following one in this issue (Botelho et al., 1978) deal with the determination of histidine pK values and with some conformational changes that can be recognized by observing histidine C-2 proton resonances in myoglobins. A group of myoglobins from 16 animal species was studied in this way (Botelho, 1975). These myoglobins offer a considerable range of variation in homologous polypeptide sequences. Within this range three cetacean families, the sperm whales, the baleen whales, and the dolphins and porpoises, are em-phasized to provide some close structural comparisons (Jones et al, 1977). The majority of the sequences of these myoglobins have been determined since the NMR data were collected and first analyzed (Botelho, 1975). Every amino acid substitution encountered so far has been found to fit qualitatively into the three-dimensional structure of sperm whale ferrimyoglobin (Watson, 1969; Takano, 1977). Between the species studied, numerous spectral and other physical similarities have been noted in the present work and in related studies (Wüthrich et al., 1970; Hartzell et al., 1968a, b; Marks et al., 1971; Friend et al., 1977). The group of myoglobin species, therefore, pro-vides a set of structurally homologous proteins that can be used