Unfolding and Translocation of Proteins Through an Alpha-Hemolysin Nanopore by ClpXP.
Methods Mol Biol
; 2186: 145-155, 2021.
Article
de En
| MEDLINE
| ID: mdl-32918735
ABSTRACT
Proteins present a significant challenge for nanopore-based sequence analysis. This is partly due to their stable tertiary structures that must be unfolded for linear translocation, and the absence of regular charge density. To address these challenges, here we describe how ClpXP, an ATP-dependent protein unfoldase, can be harnessed to unfold and processively translocate multi-domain protein substrates through an alpha-hemolysin nanopore sensor. This process results in ionic current patterns that are diagnostic of protein sequence and structure at the single-molecule level.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Endopeptidase Clp
/
Dépliement des protéines
/
Nanopores
/
Hémolysines
/
Double couche lipidique
Langue:
En
Journal:
Methods Mol Biol
Sujet du journal:
BIOLOGIA MOLECULAR
Année:
2021
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique