Determination of myoglobin stability by visible spectroscopy
Determination of myoglobin stability by visible spectroscopy
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DOI：
10.1021/ed076p1283
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发表时间：
1999-09-01
影响因子：
3
通讯作者：
Bateman, RC
中科院分区：
文献类型：
--
作者：
Sykes, PA;Shiue, HC;Bateman, RC
描述了一种用变性法测定蛋白质稳定性的简单系统。在409 nm处，肌红蛋白被异向盐盐酸胍变性，这是容易和可重复的，并且天然蛋白的稳定自由能是由变性谱的直接数学分析得出的。使用一种特性良好的蛋白质和一种廉价的程序使这一实验具有普遍的吸引力。几个补充的生物物理实验也是可能的，包括变性剂、温度或肌红蛋白来源的变化。
A simple system for the determination of protein stability by denaturation is described. The denaturation of myoglobin by the chaotropic salt guanidium hydrochloride is readily and reproducibly followed at 409 nm, and the free energy of stabilization of the native protein is derived from a straightforward mathematical analysis of the denaturation profile. The use of a well-characterized protein and an inexpensive procedure make this an attractive experiment for general use. Several complementary biophysical experiments are also possible, including the varying of denaturants, temperature, or myoglobin source.