PDZ Sample Quality Assessment by Biochemical and Biophysical Characterizations.
Biophysical techniques
Folding
Identity
PDZ domain
Protein sample
Purity
Quality control
Quantification
Stability
Structure
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2021
2021
Historique:
entrez:
20
5
2021
pubmed:
21
5
2021
medline:
22
6
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 34014518
doi: 10.1007/978-1-0716-1166-1_6
doi:
Substances chimiques
Microtubule-Associated Proteins
0
MAST2 protein, human
EC 2.7.11.1
Protein Serine-Threonine Kinases
EC 2.7.11.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
89-124Références
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