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| Line 7: |
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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=8ek4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ek4 OCA], [https://pdbe.org/8ek4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ek4 RCSB], [https://www.ebi.ac.uk/pdbsum/8ek4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ek4 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=8ek4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ek4 OCA], [https://pdbe.org/8ek4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ek4 RCSB], [https://www.ebi.ac.uk/pdbsum/8ek4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ek4 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Attaining molecular-level control over solidification processes is a crucial aspect of materials science. To control ice formation, organisms have evolved bewildering arrays of ice-binding proteins (IBPs), but these have poorly understood structure-activity relationships. We propose that reverse engineering using de novo computational protein design can shed light on structure-activity relationships of IBPs. We hypothesized that the model alpha-helical winter flounder antifreeze protein uses an unusual undertwisting of its alpha-helix to align its putative ice-binding threonine residues in exactly the same direction. We test this hypothesis by designing a series of straight three-helix bundles with an ice-binding helix projecting threonines and two supporting helices constraining the twist of the ice-binding helix. Our findings show that ice-recrystallization inhibition by the designed proteins increases with the degree of designed undertwisting, thus validating our hypothesis, and opening up avenues for the computational design of IBPs.
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| De novo designed ice-binding proteins from twist-constrained helices.,de Haas RJ, Tas RP, van den Broek D, Zheng C, Nguyen H, Kang A, Bera AK, King NP, Voets IK, de Vries R Proc Natl Acad Sci U S A. 2023 Jul 4;120(27):e2220380120. doi: , 10.1073/pnas.2220380120. Epub 2023 Jun 26. PMID:37364125<ref>PMID:37364125</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 8ek4" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
