5hfy
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Backbone Modifications in the Protein GB1 Helix: beta-2-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35== | |
| + | <StructureSection load='5hfy' size='340' side='right' caption='[[5hfy]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hfy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HFY FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=62H:(2S)-3-AMINO-2-METHYLPROPANOIC+ACID'>62H</scene>, <scene name='pdbligand=B3K:(3S)-3,7-DIAMINOHEPTANOIC+ACID'>B3K</scene>, <scene name='pdbligand=B3X:(3S)-3,5-DIAMINO-5-OXOPENTANOIC+ACID'>B3X</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hi1|5hi1]], [[5hi2|5hi2]]</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=5hfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hfy OCA], [http://pdbe.org/5hfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hfy RCSB], [http://www.ebi.ac.uk/pdbsum/5hfy PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an alpha-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in alpha-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences. | ||
| - | + | Comparison of design strategies for alpha-helix backbone modification in a protein tertiary fold.,Tavenor NA, Reinert ZE, Lengyel GA, Griffith BD, Horne WS Chem Commun (Camb). 2016 Feb 25;52(19):3789-92. doi: 10.1039/c6cc00273k. PMID:26853882<ref>PMID:26853882</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5hfy" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Griffith, B D]] | ||
| + | [[Category: Horne, W S]] | ||
| + | [[Category: Lengyel, G A]] | ||
| + | [[Category: Reinert, Z E]] | ||
| + | [[Category: Tavenor, N A]] | ||
| + | [[Category: De novo protein]] | ||
| + | [[Category: Synthetic protein]] | ||
Revision as of 18:13, 26 February 2016
Backbone Modifications in the Protein GB1 Helix: beta-2-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35
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