Footprinting of protein interactions by tritium labeling

Guillaume Mousseau; Quentin Raffy; Olivier P. Thomas; Morgane Agez; Robert Thai; Jean Philippe Renault; Serge Pin; Françoise Ochsenbein; Jean Christophe Cintrat; Bernard Rousseau

doi:10.1021/bi100031a

Footprinting of protein interactions by tritium labeling

Guillaume Mousseau, Quentin Raffy, Olivier P. Thomas, Morgane Agez, Robert Thai, Jean Philippe Renault, Serge Pin, Françoise Ochsenbein, Jean Christophe Cintrat, Bernard Rousseau

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

3 Citations (Scopus)

Abstract

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 hAsf1A_1-156 afforded data in good agreement with NMR results.

Original language	English
Pages (from-to)	4297-4299
Number of pages	3
Journal	Biochemistry
Volume	49
Issue number	20
DOIs	https://doi.org/10.1021/bi100031a
Publication status	Published - 25 May 2010
Externally published	Yes

Access to Document

10.1021/bi100031a

Cite this

@article{3b30b6950c3c4e88b624375f9ffa6ca3,

title = "Footprinting of protein interactions by tritium labeling",

abstract = "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 H3122-135 and the protein hAsf1A1-156 afforded data in good agreement with NMR results.",

author = "Guillaume Mousseau and Quentin Raffy and Thomas, \{Olivier P.\} and Morgane Agez and Robert Thai and Renault, \{Jean Philippe\} and Serge Pin and Fran{\c c}oise Ochsenbein and Cintrat, \{Jean Christophe\} and Bernard Rousseau",

year = "2010",

month = may,

day = "25",

doi = "10.1021/bi100031a",

language = "English",

volume = "49",

pages = "4297--4299",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "20",

}

TY - JOUR

T1 - Footprinting of protein interactions by tritium labeling

AU - Mousseau, Guillaume

AU - Raffy, Quentin

AU - Thomas, Olivier P.

AU - Agez, Morgane

AU - Thai, Robert

AU - Renault, Jean Philippe

AU - Pin, Serge

AU - Ochsenbein, Françoise

AU - Cintrat, Jean Christophe

AU - Rousseau, Bernard

PY - 2010/5/25

Y1 - 2010/5/25

N2 - 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 H3122-135 and the protein hAsf1A1-156 afforded data in good agreement with NMR results.

AB - 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 H3122-135 and the protein hAsf1A1-156 afforded data in good agreement with NMR results.

UR - https://www.scopus.com/pages/publications/77952632522

U2 - 10.1021/bi100031a

DO - 10.1021/bi100031a

M3 - Article

AN - SCOPUS:77952632522

SN - 0006-2960

VL - 49

SP - 4297

EP - 4299

JO - Biochemistry

JF - Biochemistry

IS - 20

ER -

Footprinting of protein interactions by tritium labeling

Abstract

Access to Document

Other files and links

Fingerprint

Cite this