書誌事項
- タイトル別名
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- Functional properties of the pseudo-distal residue in the mollusc myoglobin.
- ミオグロビン ノ キノウ ト エンイ ザンキ ノ ヤクワリ
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説明
The mollusc myoglobin possesses naturally occurring substitution at the distal E7 position (Val-E7) and its oxygen affinity is only slightly lower than those of the common mammalian myoglobins possessing the usual His E7. The structure-function relationship in this myoglobin is notexplained on the basis of the results obtained from the study of the site-directed mutation at the E7 position of mammalian myoglobin. The recent mutation, crystallographic and nuclear magnetic resonance spectroscopy studies have revealed that a guanidino NH proton of Arg E10 in the mollusc myoglobin serves as an alternative hydrogen-bond donor to the bound ligand to maintain a high ligand affinity. The functional properties of the mollusc myoglobin possessing the Val E7 are controlled by a mechanism different from that of the mammalian myoglobin possessing His E7.
収録刊行物
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- 生物物理
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生物物理 34 (1), 25-32, 1994
一般社団法人 日本生物物理学会
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詳細情報 詳細情報について
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- CRID
- 1390001206532532736
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- NII論文ID
- 110001157337
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- NII書誌ID
- AN00129693
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- ISSN
- 13474219
- 05824052
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- NDL書誌ID
- 3868114
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 使用不可