Preliminary identification of the secondary structure of the trp repressor from Escherichia coli.
Preliminary identification of the secondary structure of the trp repressor from Escherichia coli.
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大肠杆菌色氨酸阻遏蛋白二级结构的初步鉴定。
DOI：
10.1111/j.1432-1033.1985.tb09211.x
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Jardetzky,O
中科院分区：
文献类型：
--
作者：
Lane,AN;Jardetzky,O
从NMR和圆二色性测量推断了大肠杆菌色氨酸阻遏物可能的二级结构含量，并将结果与预测算法的结果进行了比较。70%的酰胺质子具有比固有速率常数小几个数量级的交换速率常数，确定它们参与氢键。交换速率常数分为两个不同的类别，一个具有20分钟的半衰期，另一个超过24小时。后一类由所有酰胺质子的50%组成，表示稳定的核。交换数据与圆二色性和预测一致，表明约55%的肽形成α螺旋，20%形成β折叠和转角。NMR谱进一步表明，几乎没有β折叠，表明二级结构类别为α。
The probable secondary structure content of the trp repressor fromEscherichia colihas been inferred from NMR and circular dichroic measurements; the results are compared wih those of prediction algorithms. 70% of the amide protons have exchange rate constants orders of magnitude smaller than the intrinsic rate constants, identifying them as participating in hydrogen bonds. The exchange rate constants fall into two distinct classes, one having half‐lives of 20 min and the other more than 24h. The latter class, consisting of 50% of all amide protons, indicates a stable core. The exchange data are consistent with circular dischroism and predictions that suggest that about 55% of the peptides form α helics, and 20% form β sheets and turns. The NMR spectrum further indicates that there is little β sheet, suggesting that the secondary structure class is α.