Titration of Apparent In-Cellula Affinities of Protein-Protein Interactions**

被引：2

作者：

Cluet, David ^{[1
]}

Vergier, Blandine ^{[1
]}

Levy, Nicolas-Pierre ^{[1
]}

Dehau, Lucie ^{[1
]}

Thurman, Alexandre ^{[1
]}

Amri, Ikram ^{[1
]}

Spichty, Martin ^{[2
]}

机构：

[1] Univ Lyon 1, Lab Biol & Modelisat Cellule, CNRS, Ecole Normale Super Lyon,Univ Lyon, 46 Allee Italie, F-69364 Lyon 07, France

[2] Univ Strasbourg, Univ Haute Alsace, Ctr Natl Rech Sci, Lab Innovat Mol & Applicat, 3 Bis Rue Alfred Werner, F-68057 Mulhouse, France

来源：

CHEMBIOCHEM | 2022年 / 23卷 / 04期

关键词：

flow cytometry; protein-protein interactions; quantitative yeast-two hybrid; single-cell analysis; GREEN FLUORESCENT PROTEIN; YEAST SURFACE 2-HYBRID; FLOW-CYTOMETRY; SYSTEM; BINDING; ASSAY; RAF; THERMODYNAMICS; BARNASE; KINASE;

D O I：

10.1002/cbic.202100640

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A genetic assay permits simultaneous quantification of two interacting proteins and their bound fraction at the single-cell level using flow cytometry. Apparent in-cellula affinities of protein-protein interactions can be extracted from the acquired data through a titration-like analysis. The applicability of this approach is demonstrated on a diverse set of interactions with proteins from different families and organisms and with in-vitro dissociation constants ranging from picomolar to micromolar.

引用

页数：5

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