Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
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...
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| Veröffentlicht in: | Nature methods 2006-02, Vol.3 (2), p.91-93 |
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| container_end_page | 93 |
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| container_title | Nature methods |
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| creator | Burz, David S Dutta, Kaushik Cowburn, David Shekhtman, Alexander |
| description | 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. |
| doi_str_mv | 10.1038/nmeth851 |
| format | Article |
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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.</description><identifier>ISSN: 1548-7091</identifier><identifier>EISSN: 1548-7105</identifier><identifier>DOI: 10.1038/nmeth851</identifier><identifier>PMID: 16432517</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Adaptor Proteins, Signal Transducing - chemistry ; Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Arabinose - pharmacology ; Ataxin-3 ; Binding Sites ; Bioinformatics ; Biological Microscopy ; Biological Techniques ; Biomedical and Life Sciences ; Biomedical Engineering/Biotechnology ; brief-communication ; Endosomal Sorting Complexes Required for Transport ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Gene Expression - drug effects ; Isopropyl Thiogalactoside - pharmacology ; Life Sciences ; Measurement ; Methods ; Models, Molecular ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; NMR ; Nuclear magnetic resonance ; Nuclear magnetic resonance spectroscopy ; Nuclear Magnetic Resonance, Biomolecular - methods ; Nuclear Proteins ; Peptide Fragments - chemistry ; Peptide Fragments - genetics ; Peptide Fragments - metabolism ; Phosphoproteins - chemistry ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Physiological aspects ; Plasmids - genetics ; Protein Binding ; Protein Conformation ; Protein Interaction Mapping - methods ; Protein Structure, Quaternary ; Protein-protein interactions ; Proteins - chemistry ; Proteins - genetics ; Proteins - metabolism ; Proteomics ; Repressor Proteins ; Spectroscopy ; Transfection ; Ubiquitin - chemistry ; Ubiquitin - genetics ; Ubiquitin - metabolism</subject><ispartof>Nature methods, 2006-02, Vol.3 (2), p.91-93</ispartof><rights>Springer Nature America, Inc. 2006</rights><rights>COPYRIGHT 2006 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Feb 2006</rights><rights>2006 Nature Publishing 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c564t-2bed1609c3363e58a44c395c001d659b682b20752f7ee4784570656e98f677493</citedby><cites>FETCH-LOGICAL-c564t-2bed1609c3363e58a44c395c001d659b682b20752f7ee4784570656e98f677493</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nmeth851$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nmeth851$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16432517$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Burz, David S</creatorcontrib><creatorcontrib>Dutta, Kaushik</creatorcontrib><creatorcontrib>Cowburn, David</creatorcontrib><creatorcontrib>Shekhtman, Alexander</creatorcontrib><title>Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)</title><title>Nature methods</title><addtitle>Nat Methods</addtitle><addtitle>Nat Methods</addtitle><description>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. 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pharmacology</subject><subject>Life Sciences</subject><subject>Measurement</subject><subject>Methods</subject><subject>Models, Molecular</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Nuclear magnetic resonance spectroscopy</subject><subject>Nuclear Magnetic Resonance, Biomolecular - methods</subject><subject>Nuclear Proteins</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - genetics</subject><subject>Peptide Fragments - metabolism</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Physiological aspects</subject><subject>Plasmids - genetics</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Interaction Mapping 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature methods</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Burz, David S</au><au>Dutta, Kaushik</au><au>Cowburn, David</au><au>Shekhtman, Alexander</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)</atitle><jtitle>Nature methods</jtitle><stitle>Nat Methods</stitle><addtitle>Nat Methods</addtitle><date>2006-02-01</date><risdate>2006</risdate><volume>3</volume><issue>2</issue><spage>91</spage><epage>93</epage><pages>91-93</pages><issn>1548-7091</issn><eissn>1548-7105</eissn><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.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>16432517</pmid><doi>10.1038/nmeth851</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Arabinose - pharmacology Ataxin-3 Binding Sites Bioinformatics Biological Microscopy Biological Techniques Biomedical and Life Sciences Biomedical Engineering/Biotechnology brief-communication Endosomal Sorting Complexes Required for Transport Escherichia coli - genetics Escherichia coli - metabolism Gene Expression - drug effects Isopropyl Thiogalactoside - pharmacology Life Sciences Measurement Methods Models, Molecular Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism NMR Nuclear magnetic resonance Nuclear magnetic resonance spectroscopy Nuclear Magnetic Resonance, Biomolecular - methods Nuclear Proteins Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - metabolism Physiological aspects Plasmids - genetics Protein Binding Protein Conformation Protein Interaction Mapping - methods Protein Structure, Quaternary Protein-protein interactions Proteins - chemistry Proteins - genetics Proteins - metabolism Proteomics Repressor Proteins Spectroscopy Transfection Ubiquitin - chemistry Ubiquitin - genetics Ubiquitin - metabolism |
| title | Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR) |
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