微尺度热泳
黄蛋白
氧化还原
凋亡诱导因子
化学
黄素组
螺旋线圈
变构调节
生物物理学
生物化学
氧化还原滴定
生物
细胞凋亡
受体
酶
程序性细胞死亡
半胱氨酸蛋白酶
有机化学
作者
Paolo Cocomazzi,Delia Tarantino,Eloise Mastrangelo,Alessandro Aliverti
出处
期刊:Methods in molecular biology
日期:2021-01-01
卷期号:: 189-198
标识
DOI:10.1007/978-1-0716-1286-6_12
摘要
To perform their action usually flavoproteins interact transiently with a variety of molecular partners, whose binding is reciprocally affected and often controlled by the redox state of the bound flavin cofactor. As a case study, here we describe an approach for the quantitative characterization of the redox-controlled interaction of the mammalian apoptosis inducing factor (AIF) with one of its known protein partners, namely, the mitochondrial coiled-coil-helix-coiled-coil-helix domain-containing protein 4 (CHCHD4). In particular, we report a protocol for the titration of the flavoprotein in both in its oxidized and reduced states with CHCHD4, using an implementation of the MicroScale Thermophoresis (MST) technique.
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