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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Publication : Methods in molecular biology (Clifton, N.J.)

Real-Time Surface Plasmon Resonance (SPR) for the Analysis of Interactions Between SUMO Traps and Mono- or PolySUMO Moieties

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Methods in molecular biology (Clifton, N.J.) - 01 Jan 2016

Xolalpa W, Rodriguez MS, England P

Link to Pubmed [PMID] – 27631800

Methods Mol. Biol. 2016;1475:99-107

Isolating endogenous SUMOylated proteins is a challenging task due to the high reversibility of this posttranslational modification. We have shown that SUMO traps are useful tools for the enrichment and isolation of proteins modified by SUMO in vitro and in vivo. To characterize the affinity and specificity of different SUMO chains for these traps, that are based on SUMO-interacting motifs, we have used real-time surface plasmon resonance (SPR), which allows a label-free analysis of protein/protein interactions. Here, a protocol to determine the affinities of multivalent SUMO traps for polySUMO chains or mono-SUMO molecules by SPR is presented.

https://www.ncbi.nlm.nih.gov/pubmed/27631800