Baseline length and automated fitting of denaturation data
Baseline length and automated fitting of denaturation data
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DOI：
10.1002/pro.5560070524
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发表时间：
1998-05-01
期刊：
影响因子：
8
通讯作者：
Pielak, GJ
中科院分区：
文献类型：
--
作者：
Allen, DL;Pielak, GJ
为了了解蛋白质序列和稳定性之间的关系，我们经常比较来自不同蛋白质的数据，这些蛋白质的数据仅由一个氨基酸取代。通常，氨基酸的变化会导致协同变性转变转移到较低的温度，从而减少来自天然状态的信号。在这里，我们表明，明显的稳定性变化，即，变性的自由能Δ G（D）也可以由转变的低温端的点的缺乏引起。此外，我们提出了一种方法来克服这个问题。
To understand relationships between protein sequence and stability, we often compare data from proteins that differ by the substitution of one amino acid. Frequently, an amino acid change causes the cooperative denaturation transitions to shift to lower temperatures, diminishing the signal from the native state. Here we show that apparent stability changes, i.e., the free energy of denaturation, Delta G(D), can also be caused by a deficiency of points in the low temperature end of the transition. In addition, we suggest a method for overcoming this problem.