5bvl: Difference between revisions

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</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=5bvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bvl OCA], [http://pdbe.org/5bvl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bvl RCSB], [http://www.ebi.ac.uk/pdbsum/5bvl PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Despite efforts for over 25 years, de novo protein design has not succeeded in achieving the TIM-barrel fold. Here we describe the computational design of four-fold symmetrical (beta/alpha)8 barrels guided by geometrical and chemical principles. Experimental characterization of 33 designs revealed the importance of side chain-backbone hydrogen bonds for defining the strand register between repeat units. The X-ray crystal structure of a designed thermostable 184-residue protein is nearly identical to that of the designed TIM-barrel model. PSI-BLAST searches do not identify sequence similarities to known TIM-barrel proteins, and sensitive profile-profile searches indicate that the design sequence is distant from other naturally occurring TIM-barrel superfamilies, suggesting that Nature has sampled only a subset of the sequence space available to the TIM-barrel fold. The ability to design TIM barrels de novo opens new possibilities for custom-made enzymes.

De novo design of a four-fold symmetric TIM-barrel protein with atomic-level accuracy.,Huang PS, Feldmeier K, Parmeggiani F, Fernandez Velasco DA, Hocker B, Baker D Nat Chem Biol. 2015 Nov 23. doi: 10.1038/nchembio.1966. PMID:26595462<ref>PMID:26595462</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 5: / Line 5: @@
 </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=5bvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bvl OCA], [http://pdbe.org/5bvl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bvl RCSB], [http://www.ebi.ac.uk/pdbsum/5bvl PDBsum]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Despite efforts for over 25 years, de novo protein design has not succeeded in achieving the TIM-barrel fold. Here we describe the computational design of four-fold symmetrical (beta/alpha)8 barrels guided by geometrical and chemical principles. Experimental characterization of 33 designs revealed the importance of side chain-backbone hydrogen bonds for defining the strand register between repeat units. The X-ray crystal structure of a designed thermostable 184-residue protein is nearly identical to that of the designed TIM-barrel model. PSI-BLAST searches do not identify sequence similarities to known TIM-barrel proteins, and sensitive profile-profile searches indicate that the design sequence is distant from other naturally occurring TIM-barrel superfamilies, suggesting that Nature has sampled only a subset of the sequence space available to the TIM-barrel fold. The ability to design TIM barrels de novo opens new possibilities for custom-made enzymes.
+De novo design of a four-fold symmetric TIM-barrel protein with atomic-level accuracy.,Huang PS, Feldmeier K, Parmeggiani F, Fernandez Velasco DA, Hocker B, Baker D Nat Chem Biol. 2015 Nov 23. doi: 10.1038/nchembio.1966. PMID:26595462<ref>PMID:26595462</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5bvl" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>