1rh4: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh4 OCA], [https://pdbe.org/1rh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh4 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh4 ProSAT]</span></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=1rh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh4 OCA], [https://pdbe.org/1rh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh4 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail. | |||
High-resolution protein design with backbone freedom.,Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS Science. 1998 Nov 20;282(5393):1462-7. PMID:9822371<ref>PMID:9822371</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1rh4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 03:26, 21 November 2024
RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMERRH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER
Structural highlights
Publication Abstract from PubMedRecent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail. High-resolution protein design with backbone freedom.,Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS Science. 1998 Nov 20;282(5393):1462-7. PMID:9822371[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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