蛋白質におけるアスパラギン酸の異性化
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概要
- 論文の詳細を見る
Aspartic acid in protein isomerizes autocatalytically to isoaspartate <I>via</I> succinimide intermediate <I>in vitro</I> and <I>in vivo</I>. We have determined the crystal structures of <I>Ustilago sphaerogena</I> ribonuclease U<SUB>2</SUB> with an isoaspartate residue and hen egg-white lysozymes with a succinimide intermediate and with an isoaspartate residue at 1.8 Å resolution. These crystal structures reveal that the isomerizations of aspartic acids induce structural changes on proteins, which result in modifying the function and physical properties of the proteins.
- 日本結晶学会の論文
- 1998-08-28
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