Large Flexibility of Dihydrofolate Reductase as Revealed by Temperature Effects on the Volume and Compressibility
Large Flexibility of Dihydrofolate Reductase as Revealed by Temperature Effects on the Volume and Compressibility
复制标题
温度对体积和压缩性的影响揭示了二氢叶酸还原酶的巨大灵活性
DOI：
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发表时间：
1999
期刊：
影响因子：
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通讯作者：
K. Gekko
中科院分区：
文献类型：
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作者：
T. Kamiyama;E. Ohmae;K. Gekko
随着温度的升高，大肠杆菌二氢叶酸还原酶（DHFR）的部分比容和绝热压缩系数显著增加，这与光谱测量所揭示的构象变化相对应.这些结果表明，该蛋白质在天然状态下具有高度柔性的结构，其三级结构或疏水核心容易随温度膨胀以产生内部空腔。
The partial specific volume and adiabatic compressibility of dihydrofolate reductase (DHFR) from Escherichia coli remarkably increased as temperature was higher, corresponding to the conformational changes as revealed by spectroscopic measurements. These results demonstrate that this protein has a highly flexible structure at the native state whose tertiary structure or hydrophobic core is easily expanded with temperature to produce the internal cavities.
影响因子：
2.9
作者：
Sawaya, MR;Kraut, J
通讯作者：
Kraut, J