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

Chemistry

University at Albany

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

153 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

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title = "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.",

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

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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.

UR - https://www.scopus.com/pages/publications/31744435251

U2 - 10.1038/nmeth851

DO - 10.1038/nmeth851

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VL - 3

SP - 91

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JO - Nature Methods

JF - Nature Methods

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ER -

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

Abstract

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