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Updated: Aug 13, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
David S Burz1, Kaushik Dutta, David Cowburn
1State University of New York at Albany, Department of Chemistry, 1400 Washington Ave., Albany, New York 12222, USA.
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.
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