Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR).
We describe a high-throughput in-cell nuclear magnetic resonance (NMR)-based method for mapping the structural changes that accompany protein-protein interactions (STINT-NMR). The method entails sequentially expressing two (or more) proteins within a single bacterial cell in a time-controlled manner and monitoring the protein interactions using in-cell NMR spectroscopy. The resulting spectra ... provide a complete titration of the interaction and define structural details of the interacting surfaces at atomic resolution.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Arabinose, Binding Sites, Endosomal Sorting Complexes Required for Transport, Escherichia coli, Gene Expression, Isopropyl Thiogalactoside, Models, Molecular, Nerve Tissue Proteins, Nuclear Magnetic Resonance, Biomolecular, Nuclear Proteins, Peptide Fragments, Phosphoproteins, Plasmids, Protein Binding, Protein Conformation, Protein Interaction Mapping, Protein Structure, Quaternary, Proteins, Repressor Proteins, Transfection, Ubiquitin
Adaptor Proteins, Signal Transducing, Arabinose, Binding Sites, Endosomal Sorting Complexes Required for Transport, Escherichia coli, Gene Expression, Isopropyl Thiogalactoside, Models, Molecular, Nerve Tissue Proteins, Nuclear Magnetic Resonance, Biomolecular, Nuclear Proteins, Peptide Fragments, Phosphoproteins, Plasmids, Protein Binding, Protein Conformation, Protein Interaction Mapping, Protein Structure, Quaternary, Proteins, Repressor Proteins, Transfection, Ubiquitin
Nat. Methods
Date: Feb. 01, 2006
PubMed ID: 16432517
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