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4uzm

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uzm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uzm RCSB], [http://www.ebi.ac.uk/pdbsum/4uzm PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uzm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uzm RCSB], [http://www.ebi.ac.uk/pdbsum/4uzm PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have previously reported a phage display method for the identification of protein domains on a genome-wide scale (shotgun proteolysis). Here we present the solution structure of a fragment of the Escherichia coli membrane protein yrfF, as identified by shotgun proteolysis, and determined by NMR spectroscopy. Despite the absence of computational predictions, the fragment formed a well-defined beta-barrel structure, distantly falling within the OB-fold classification. Our results highlight the potential of high-throughput experimental approaches for the identification of protein domains for structural studies.
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Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis.,Allen MD, Christie M, Jones P, Porebski BT, Roome B, Freund SM, Buckle AM, Bycroft M, Christ D Protein Eng Des Sel. 2015 Apr 15. pii: gzv021. PMID:25877662<ref>PMID:25877662</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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Revision as of 05:46, 30 April 2015

Shotgun proteolysis: A practical application

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