1btd

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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:1btd.png|left|200px]]
 
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==BETADOUBLET: DE NOVO DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A MODEL BETASANDWICH PROTEIN==
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The line below this paragraph, containing "STRUCTURE_1btd", creates the "Structure Box" on the page.
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<StructureSection load='1btd' size='340' side='right'caption='[[1btd]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1btd FirstGlance], [https://www.ebi.ac.uk/pdbsum/1btd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btd ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1btd| PDB=1btd | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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How an amino acid sequence encodes the information necessary for a protein to adopt a unique tertiary structure remains unresolved. We are addressing this problem by designing "from scratch" protein molecules that will adopt predetermined three-dimensional structures. Based on this strategy, two identical four-stranded beta-sheets were designed to dimerize and form a beta-sandwich protein, called betadoublet. A synthetic gene encoding half the beta-sandwich protein was expressed in Escherichia coli, and the protein was purified to homogeneity. Biophysical characterization of betadoublet in aqueous solution demonstrated that the disulfide formed between the two sheets and that the dimer was a compact unaggregated globular protein, consisting predominantly of beta-sheet and stable to thermal denaturation. It has some backbone amide protons whose exchange is slow enough to be measured by NMR but binds more of the dye 1-anilinonaphthalene-8-sulfonate than a well-folded protein.
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===BETADOUBLET: DE NOVO DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A MODEL BETASANDWICH PROTEIN===
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Betadoublet: de novo design, synthesis, and characterization of a beta-sandwich protein.,Quinn TP, Tweedy NB, Williams RW, Richardson JS, Richardson DC Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):8747-51. PMID:8090717<ref>PMID:8090717</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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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_8090717}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1btd" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 8090717 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8090717}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTD OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:8090717</ref><references group="xtra"/>
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[[Category: Quinn, T P]]
[[Category: Quinn, T P]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 06:44:06 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

BETADOUBLET: DE NOVO DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A MODEL BETASANDWICH PROTEIN

PDB ID 1btd

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