Solution structure of insect CSP and OBPs by NMR.
CSP-sg4 structure
Insect CSP
Insect OBP
Protein NMR
Journal
Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271
Informations de publication
Date de publication:
2020
2020
Historique:
entrez:
24
8
2020
pubmed:
24
8
2020
medline:
24
6
2021
Statut:
ppublish
Résumé
Insect odorant binding proteins (OBPs) and chemosensory proteins (CSPs) are proteins deputed to the solubilization, transport and stabilization of lipophilic and odorant compounds. These proteins have a conserved fold, which undergoes massive structural rearrangements in order to accommodate medium to large-sized lipophilic ligands. Solution NMR spectroscopy, due to its intrinsically dynamic nature, is the perfect technique to extrapolate structural information and dynamic parameters and to elucidate the conformational changes that occur upon ligand binding. This chapter will describe in detail the experimental protocols for the production and purification of isotope-labeled recombinant CSPs and OBPs for NMR studies. Detailed procedures for spectra acquisition, processing and analysis will be presented, focusing on the protein CSP-sg4 from Schistocerca gregaria as a model. Finally, experiments aimed at providing information on protein flexibility and ligand binding modes will also be described.
Identifiants
pubmed: 32828252
pii: S0076-6879(20)30191-9
doi: 10.1016/bs.mie.2020.04.063
pii:
doi:
Substances chimiques
Insect Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
169-192Informations de copyright
© 2020 Elsevier Inc. All rights reserved.