Probing the mechanism of the peroxiredoxin decamer interaction with its reductase sulfiredoxin from the single molecule to the solution scale-Reference-Cited by-同舟云学术

Probing the mechanism of the peroxiredoxin decamer interaction with its reductase sulfiredoxin from the single molecule to the solution scale

Published:2022 Issue:5 Volume:7 Page:515-525
ISSN:2055-6756
Container-title:Nanoscale Horizons
language:en
Short-container-title:Nanoscale Horiz.

Author:

Beaussart Audrey¹^ORCID,Canonico Florent²,Mazon Hortense²,Hidalgo Jorge²,Cianférani Sarah³⁴^ORCID,Le Cordier Hélène²,Kriznik Alexandre²⁵^ORCID,Rahuel-Clermont Sophie²⁵^ORCID

Affiliation:

1. Université de Lorraine, CNRS, LIEC, F-54000 Nancy, France

2. Université de Lorraine, CNRS, IMoPA, F-54000 Nancy, France

3. Laboratoire de Spectrométrie de Masse BioOrganique, Université de Strasbourg, CNRS, IPHC UMR 7178, 67000 Strasbourg, France

4. Infrastructure Nationale de Protéomique ProFI – FR2048 CNRS CEA, 67087 Strasbourg, France

5. Université de Lorraine, CNRS, INSERM, UMS2008 IBSLor, Biophysics and Structural Biology core facility, F-54000 Nancy, France

Abstract

A multiscale strategy based on AFM, native mass spectrometry and bulk solution techniques correlates affinity, kinetics, and single molecule data to understand regulation of the multivalent interaction of a decameric protein with its partner.

Funder

Agence Nationale de la Recherche

Ligue Contre le Cancer

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science

Link

http://pubs.rsc.org/en/content/articlepdf/2022/NH/D2NH00037G

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