| Autor: |
Caillet-Saguy C; Institut Pasteur, Unité Récepteurs-Canaux, CNRS UMR 3571, Paris, France., Brûlé S; Institut Pasteur, Plate-forme de Biophysique Moléculaire, CNRS UMR 3528, Paris, France., Wolff N; Institut Pasteur, Unité Récepteurs-Canaux, CNRS UMR 3571, Paris, France. nicolas.wolff@pasteur.fr., Raynal B; Institut Pasteur, Plate-forme de Biophysique Moléculaire, CNRS UMR 3528, Paris, France. |
| Abstrakt: |
PDZ domains are small globular domains involved in protein-protein interactions. They participate in a wide range of critical cellular processes. These domains, very abundant in the human proteome, are widely studied by high-throughput interactomics approaches and by biophysical and structural methods. However, the quality of the results is strongly related to the optimal folding and solubility of the domains. We provide here a detailed description of protocols for a strict quality assessment of the PDZ constructs. We describe appropriate experimental approaches that have been selected to overcome the small size of such domains to check the purity, identity, homogeneity, stability, and folding of samples. |
