A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
J Biomol NMR
; 50(3): 229-36, 2011 Jul.
Article
em En
| MEDLINE
| ID: mdl-21626214
ABSTRACT
Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance assignment of methyl probes in high molecular weight protein assemblies can be efficiently achieved by combining fast NMR experiments, residue-type-specific isotope-labeling and automated site-directed mutagenesis. The utility of this general and straightforward strategy is demonstrated through the characterization of intermolecular interactions involving a 468-kDa multimeric aminopeptidase, PhTET2.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Mutagênese Sítio-Dirigida
/
Ressonância Magnética Nuclear Biomolecular
Idioma:
En
Revista:
J Biomol NMR
Assunto da revista:
BIOLOGIA MOLECULAR
/
DIAGNOSTICO POR IMAGEM
/
MEDICINA NUCLEAR
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
França