Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)

David S. Burz; Kaushik Dutta; David Cowburn; Alexander Shekhtman

doi:10.1038/nmeth851

Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)

David S. Burz, Kaushik Dutta, David Cowburn, Alexander Shekhtman

Research output: Contribution to journal › Article › peer-review

148 Scopus citations

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.

Original language	English
Pages (from-to)	91-93
Number of pages	3
Journal	Nature Methods
Volume	3
Issue number	2
DOIs	https://doi.org/10.1038/nmeth851
State	Published - Feb 2006
Externally published	Yes

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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.",

author = "Burz, {David S.} and Kaushik Dutta and David Cowburn and Alexander Shekhtman",

note = "Funding Information: This work was supported by grants to A.S. (American Diabetes Association Career Development Award 1-06-CD-23) and to D.C. (National Institutes of Health 2R01GM047021-13A2).",

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AU - Burz, David S.

AU - Dutta, Kaushik

AU - Cowburn, David

AU - Shekhtman, Alexander

N1 - Funding Information: This work was supported by grants to A.S. (American Diabetes Association Career Development Award 1-06-CD-23) and to D.C. (National Institutes of Health 2R01GM047021-13A2).

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N2 - 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.

AB - 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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Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)

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