STRUCTURE OF LACTATE DEHYDROGENASE AT 2.8A RESOLUTION
STRUCTURE OF LACTATE DEHYDROGENASE AT 2.8A RESOLUTION
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DOI：
10.1038/2271098a0
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发表时间：
1970-01-01
期刊：
影响因子：
64.8
通讯作者：
WONACOTT, AJ
中科院分区：
文献类型：
--
作者：
ADAMS, MJ;FORD, GC;WONACOTT, AJ
乳酸脱氢酶M4同工酶的电子密度分布揭示了亚基的构象、亚基之间的边界以及与辅酶和底物结合有关的特征。
Electron density distributions for the M4isoenzyme of LDH reveal details of the conformation of the subunit, boundaries between the subunits, and features relevant to the binding of coenzyme and substrate.