Nature Methods 3, 91 - 93 (2006)
Published online: 23 January 2006; | doi:10.1038/nmeth851
Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)David S Burz1, Kaushik Dutta2, David Cowburn2
& Alexander Shekhtman11
State University of New York at Albany, Department of Chemistry, 1400 Washington Ave., Albany, New York 12222, USA. 2
New York Structural Biology Center, 89 Convent Avenue, Park Building at 133rd St., New York, New York 10027, USA.
Correspondence should be addressed to Alexander Shekhtman ashekhta@albany.edu 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.
MORE ARTICLES LIKE THIS These links to content published by NPG are automatically generated.
|
