| Literature DB >> 16432517 |
David S Burz1, Kaushik Dutta, David Cowburn, Alexander Shekhtman.
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.Mesh:
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Year: 2006 PMID: 16432517 PMCID: PMC4447212 DOI: 10.1038/nmeth851
Source DB: PubMed Journal: Nat Methods ISSN: 1548-7091 Impact factor: 28.547