通过微量热泳动（MST）测量FNR-NrdI相互作用
Measurement of FNR-NrdI Interaction by Microscale Thermophoresis (MST).
作者信息
Gudim Ingvild, Lofstad Marie, Hammerstad Marta, Hersleth Hans-Petter
机构信息
Department of Biosciences, University of Oslo, Oslo, Norway.
Department of Chemistry, University of Oslo, Oslo, Norway.
出版信息
Bio Protoc. 2017 Apr 20;7(8):e2223. doi: 10.21769/BioProtoc.2223.
This protocol describes how to measure protein-protein interactions by microscale thermophoresis (MST) using the Monolith NT.115 instrument (NanoTemper). We have used the protocol to determine the binding affinities between three different flavodoxin reductases (FNRs) and a flavodoxin-like protein, NrdI, from ( Lofstad , 2016 ). NrdI is essential in the activation of the manganese-bound form of the class Ib ribonucleotide reductase (RNR) system. RNRs, in turn, are the only source of the synthesis of deoxyribonucleotides required for DNA replication and repair in all living organisms.
本方案描述了如何使用Monolith NT.115仪器（NanoTemper）通过微量热泳（MST）测量蛋白质-蛋白质相互作用。我们已使用该方案确定了三种不同的黄素氧还蛋白还原酶（FNR）与一种来自[罗夫斯塔德，2016]的类黄素氧还蛋白NrdI之间的结合亲和力。NrdI在激活Ib类核糖核苷酸还原酶（RNR）系统的锰结合形式中至关重要。反过来，RNR是所有生物体DNA复制和修复所需脱氧核糖核苷酸合成的唯一来源。
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