Department of Biochemistry and Molecular Biology, Virginia Commonwealth University, Richmond, VA 23298, USA.
Anal Biochem. 2010 Dec 15;407(2):278-80. doi: 10.1016/j.ab.2010.08.019. Epub 2010 Aug 21.
We have demonstrated that an approach using guanidine hydrochloride at low concentrations to progressively disrupt protein-protein interactions can be quantitated using dynamic light scattering. This approach is sensitive enough to detect ligand-induced changes of subunit-subunit interactions for homo-hexameric glutamate dehydrogenase, allowing ΔΔG of reversible subunit dissociation to be calculated. The use of dynamic light scattering makes this approach generally applicable to soluble proteins to monitor the relative strength of protein-protein interactions with a particular emphasis on assessing the impact of ligand binding on such interfaces.
我们已经证明，使用低浓度盐酸胍逐渐破坏蛋白质-蛋白质相互作用的方法可以使用动态光散射进行定量。这种方法足够灵敏，可以检测同六聚体谷氨酸脱氢酶的亚基-亚基相互作用的配体诱导变化，从而可以计算可逆亚基解离的 ΔΔG。动态光散射的使用使这种方法广泛适用于可溶性蛋白质，以监测蛋白质-蛋白质相互作用的相对强度，特别强调评估配体结合对这些界面的影响。
