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

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.

SUBMITTER: Burz DS

PROVIDER: S-EPMC4447212 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature

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

Burz David S DS Dutta Kaushik K Cowburn David D Shekhtman Alexander A

Nature methods 20060201 2

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 ...[more]

PMID: 16432517

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| S-EPMC3796943 | biostudies-literature

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