Literature DB >> 16432517

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

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.

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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


  15 in total

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9.  A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins.

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Journal:  Biochem Biophys Res Commun       Date:  2002-09-06       Impact factor: 3.575

10.  STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes.

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Journal:  J Biol Chem       Date:  2003-01-27       Impact factor: 5.157

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  55 in total

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Journal:  Nat Protoc       Date:  2010-05-13       Impact factor: 13.491

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Review 3.  Biological synthesis of circular polypeptides.

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Review 4.  A Unique Tool for Cellular Structural Biology: In-cell NMR.

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5.  Ribosome Mediated Quinary Interactions Modulate In-Cell Protein Activities.

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Review 7.  Site-specific labeling of proteins with NMR-active unnatural amino acids.

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8.  Controlling and quantifying protein concentration in Escherichia coli.

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Review 9.  In-Cell NMR Spectroscopy of Intrinsically Disordered Proteins.

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10.  Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells.

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