盐酸胍亚变性极限下的蛋白质硬化与熵稳定化
Protein stiffening and entropic stabilization in the subdenaturing limit of guanidine hydrochloride.
作者信息
Kumar Rajesh, Prabhu N Prakash, Yadaiah M, Bhuyan Abani K
机构信息
School of Chemistry, University of Hyderabad, Hyderabad 500 046, India.
出版信息
Biophys J. 2004 Oct;87(4):2656-62. doi: 10.1529/biophysj.104.044701.
Abstract
Subdenaturing concentrations of guanidine hydrochloride (GdnHCl) stabilize proteins. For ferrocytochrome c the stabilization is detected at subglobal level with no measured change in global stability. These deductions are made by comparing observed rates of thermally driven ferrocytochrome cHCO reactions with global unfolding rates of ferrocytochrome c measured by stopped flow and NMR hydrogen exchange in the presence of a wide range of GdnHCl concentrations at pH 7, 22 degrees C.
摘要
亚变性浓度的盐酸胍（GdnHCl）可使蛋白质稳定。对于亚铁细胞色素c，在亚整体水平检测到了这种稳定性，而整体稳定性没有测量到变化。这些推论是通过比较在pH 7、22℃下，在广泛的GdnHCl浓度存在下，热驱动的亚铁细胞色素cHCO反应的观察速率与通过停流和核磁共振氢交换测量的亚铁细胞色素c的整体解折叠速率得出的。
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