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Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR).
- Source :
-
Nature methods [Nat Methods] 2006 Feb; Vol. 3 (2), pp. 91-3. - Publication Year :
- 2006
-
Abstract
- 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.
- Subjects :
- Adaptor Proteins, Signal Transducing chemistry
Adaptor Proteins, Signal Transducing genetics
Adaptor Proteins, Signal Transducing metabolism
Arabinose pharmacology
Ataxin-3
Binding Sites
Endosomal Sorting Complexes Required for Transport
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression drug effects
Isopropyl Thiogalactoside pharmacology
Models, Molecular
Nerve Tissue Proteins chemistry
Nerve Tissue Proteins genetics
Nerve Tissue Proteins metabolism
Nuclear Proteins
Peptide Fragments chemistry
Peptide Fragments genetics
Peptide Fragments metabolism
Phosphoproteins chemistry
Phosphoproteins genetics
Phosphoproteins metabolism
Plasmids genetics
Protein Binding
Protein Conformation
Proteins chemistry
Proteins genetics
Proteins metabolism
Repressor Proteins
Transfection
Ubiquitin chemistry
Ubiquitin genetics
Ubiquitin metabolism
Nuclear Magnetic Resonance, Biomolecular methods
Protein Interaction Mapping methods
Protein Structure, Quaternary
Subjects
Details
- Language :
- English
- ISSN :
- 1548-7091
- Volume :
- 3
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Nature methods
- Publication Type :
- Academic Journal
- Accession number :
- 16432517
- Full Text :
- https://doi.org/10.1038/nmeth851