The structures of deoxy human haemoglobin and the mutant Hb Tyra42His at 120 K

Jeremy R. H. Tame; Beatrice Vallone

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The structures of deoxy human haemoglobin and the mutant Hb Tyra42His at 120 K

机译：人类脱氧血红蛋白的结构和突变Hb Tyra42His在120 K

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The structures of deoxy human haemoglobin and an artificial mutant (Tyrα42 → His) have been solved at 120 K. While overall agreement between these structures and others in the PDB is very good, certain side chains are found to be shifted, absent from the electron-density map or in different rotamers. Non-crystallographic symmetry (NCS) is very well obeyed in the native protein, but not around the site of the changed residue in the mutant. NCS is also not obeyed by the water molecule invariably found in the α-chain haem pocket in room-temperature crystal structures of haemoglobin. At 120 K, this water molecule disappears from one α chain in the asymmetric unit but not the other.

机译：人类脱氧血红蛋白的结构和一个人工突变体(酪氨酸α42→他)已经解决在120 K。结构和其他PDB很好,发现某些侧链转移,从电子密度图或缺席不同的旋转异构体。(nc)很好遵守本机蛋白质,但不是在网站改变了残留的突变体。分子总是在α链血红素口袋在室温的晶体结构血红蛋白。从一个不对称的α链消失单位而不是其他。

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《Acta crystallographica.Section D. Biological crystallography》 |2000年第7期|805-811|共7页
作者
Jeremy R. H. Tame; Beatrice Vallone;
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作者单位

Dipartimento di Scienze Biochimiche, Universita di Roma `La Sapienza', Piazzale A. Moro, 5 00185 Roma, Italy;

Protonic Nanomachine Project, ERATO, 3-4 Hikaridai, Seika, Kyoto 619-0237, Japan;

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正文语种英语
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关键词
Mutants; Water Molecule; electron density mapHemoglobins;

机译：突变体,水分子,电子密度;

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The structures of deoxy human haemoglobin and the mutant Hb Tyra42His at 120 K

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