期刊
JOURNAL OF BIOMOLECULAR NMR
卷 50, 期 3, 页码 229-236出版社
SPRINGER
DOI: 10.1007/s10858-011-9513-5
关键词
NMR spectroscopy; High molecular weight proteins; Assignment; Site-specific mutagenesis; Methyl-group labeling
资金
- CONACYT
- CNRS
- Agence Nationale de la Recherche [ANR-09-PIRIBio-445583, ANR-07-BLAN-0085]
- Agence Nationale de la Recherche (ANR) [ANR-07-BLAN-0085] Funding Source: Agence Nationale de la Recherche (ANR)
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.
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