Footprinting of Protein Interactions by Tritium Labeling

被引：2

作者：

Mousseau, Guillaume ^{[1
]}

Raffy, Quentin ^{[2
]}

Thomas, Oliver P. ^{[1
]}

Agez, Morgane ^{[1
]}

Thai, Robert ^{[1
]}

Renault, Jean Philippe ^{[2
]}

Pin, Serge ^{[2
,3
]}

Ochsenbein, Francoise ^{[1
,4
]}

Cintrat, Jean-Christophe ^{[1
]}

Rousseau, Bernard ^{[1
]}

机构：

[1] CEA, IBITECS, F-91191 Gif Sur Yvette, France

[2] CEA, IRAMIS, F-91191 Gif Sur Yvette, France

[3] CEA, URA 331, Lab Claude Frejacques, CNRS, F-91191 Gif Sur Yvette, France

[4] CEA, URA Syst Membranaires Photobiol Stress & Detoxica, F-91191 Gif Sur Yvette, France

来源：

BIOCHEMISTRY | 2010年 / 49卷 / 20期

关键词：

EXCHANGE-MASS-SPECTROMETRY; HISTONE CHAPERONE ASF1; STRUCTURAL PROTEOMICS; DYNAMICS; INTERFACES; RADIOLYSIS; PROBE;

D O I：

10.1021/bi100031a

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 new footprinting method for mapping protein interactions has been developed, using tritium as a radioactive label. As residues involved in an interaction are less labeled when the complex is formed, they can be identified via comparison of the tritium incorporation of each residue of the bound protein with that of the unbound one. Application of this footprinting method to the complex formed by the histone H3 fragment H3(122-135) and the protein hAsflA(1-156) afforded data in good agreement with NMR results.

引用

页码：4297 / 4299

页数：3

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