Solution structure of insect CSP and OBPs by 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
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

169-192

Informations de copyright

© 2020 Elsevier Inc. All rights reserved.

Auteurs

Serena Leone (S)

Department of Chemical Sciences, University of Naples "Federico II", Complesso Universitario Monte S. Angelo, Napoli, Italy.

Alessandro Emendato (A)

Department of Chemical Sciences, University of Naples "Federico II", Complesso Universitario Monte S. Angelo, Napoli, Italy.

Roberta Spadaccini (R)

Department of Science and Technology, Università degli Studi del Sannio, Benevento, Italy.

Delia Picone (D)

Department of Chemical Sciences, University of Naples "Federico II", Complesso Universitario Monte S. Angelo, Napoli, Italy. Electronic address: delia.picone@unina.it.

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Classifications MeSH