EaStCHEM School of Chemistry, Biomedical Sciences Research Complex and Centre of Magnetic resonance, University of St Andrews, North Haugh, St Andrews, KY16 9ST, Scotland, UK.
Chem Commun (Camb). 2022 Aug 4;58(63):8790-8793. doi: 10.1039/d2cc02360a.
Protein interaction studies often require very low concentrations and highly sensitive biophysical methods. Here, we demonstrate that pulse dipolar electron paramagnetic resonance spectroscopy allows measuring dissociation constants in the nanomolar range. This approach is appealing for concentration-limited biomolecular systems and medium-to-high-affinity binding studies, demonstrated here at 50 nanomolar protein concentration.
蛋白质相互作用研究通常需要非常低的浓度和高度灵敏的生物物理方法。在这里，我们证明了脉冲偶极电子顺磁共振波谱法允许在纳摩尔范围内测量离解常数。这种方法适用于浓度有限的生物分子系统和中高亲和力结合研究，在 50 纳摩尔蛋白质浓度下得到了证明。
