Fast NMR method to probe solvent accessibility and disordered regions in proteins.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
07 02 2019
07 02 2019
Historique:
received:
09
05
2018
accepted:
10
12
2018
entrez:
9
2
2019
pubmed:
9
2
2019
medline:
23
9
2020
Statut:
epublish
Résumé
Understanding protein structure and dynamics, which govern key cellular processes, is crucial for basic and applied research. Intrinsically disordered protein (IDP) regions display multifunctionality via alternative transient conformations, being key players in disease mechanisms. IDP regions are abundant, namely in small viruses, allowing a large number of functions out of a small proteome. The relation between protein function and structure is thus now seen from a different perspective: as IDP regions enable transient structural arrangements, each conformer can play different roles within the cell. However, as IDP regions are hard and time-consuming to study via classical techniques (optimized for globular proteins with unique conformations), new methods are required. Here, employing the dengue virus (DENV) capsid (C) protein and the immunoglobulin-binding domain of streptococcal protein G, we describe a straightforward NMR method to differentiate the solvent accessibility of single amino acid N-H groups in structured and IDP regions. We also gain insights into DENV C flexible fold region biological activity. The method, based on minimal pH changes, uses the well-established
Identifiants
pubmed: 30733478
doi: 10.1038/s41598-018-37599-z
pii: 10.1038/s41598-018-37599-z
pmc: PMC6367444
doi:
Substances chimiques
Bacterial Proteins
0
Capsid Proteins
0
IgG Fc-binding protein, Streptococcus
0
Intrinsically Disordered Proteins
0
Solvents
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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