STUDIES OF COMPLETELY DEUTERIATED PROTEINS .2. THERMAL DENATURATION IN D2O
STUDIES OF COMPLETELY DEUTERIATED PROTEINS .2. THERMAL DENATURATION IN D2O
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DOI：
10.1021/bi00906a033
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发表时间：
1963-01-01
期刊：
影响因子：
2.9
通讯作者：
BERNS, DS
中科院分区：
文献类型：
--
作者：
BERNS, DS
完全氘化的蛋白质及其氢类似物在缓冲D2O中的热变性研究表明，氘化蛋白质总是在比其氢类似物更低的温度下变性。在D2O和H2O中热变性的交叉比较不能给出一个简单的容易解释的图像。然而，所有的结果是一致的建议，内旋转是一个重要的因素，在确定蛋白质结构。
Thermal denaturation studies of a fully deuteriated protein and its hydrogen analog in buffered D2O demonstrate that the deuterio protein always denatures at a lower temperature than its hydrogen analog. Cross comparisons of thermal denaturation in D2O and H2O do not give a simple easily interpreted picture. All results are, however, consistent with the suggestion that internal rotation is an important factor in the determination of protein structure.