5hg2: Difference between revisions

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'''Unreleased structure'''


The entry 5hg2 is ON HOLD  until Paper Publication
==Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-2-Asn35==
<StructureSection load='5hg2' size='340' side='right' caption='[[5hg2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hg2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HG2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2N:(2S)-4-AMINO-2-(AMINOMETHYL)-4-OXOBUTANOIC+ACID'>B2N</scene>, <scene name='pdbligand=B3A:(3S)-3-AMINOBUTANOIC+ACID'>B3A</scene>, <scene name='pdbligand=B3K:(3S)-3,7-DIAMINOHEPTANOIC+ACID'>B3K</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">[[5hfy|5hfy]], [[5hi1|5hi1]]</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=5hg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hg2 OCA], [http://pdbe.org/5hg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hg2 RCSB], [http://www.ebi.ac.uk/pdbsum/5hg2 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.


Authors: Tavenor, N.A., Reinert, Z.E., Lengyel, G.A., Griffith, B.D., Horne, W.S.
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>


Description: Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-2-Asn35
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Reinert, Z.E]]
<div class="pdbe-citations 5hg2" style="background-color:#fffaf0;"></div>
[[Category: Griffith, B.D]]
== References ==
[[Category: Horne, W.S]]
<references/>
[[Category: Lengyel, G.A]]
__TOC__
[[Category: Tavenor, N.A]]
</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]]
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