5hi1: Difference between revisions
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==Backbone Modifications in the Protein GB1 Helix: Aib24, beta-3-Lys28, beta-3-Lys31, Aib35== | |||
<StructureSection load='5hi1' size='340' side='right'caption='[[5hi1]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hi1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HI1 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=B3K:(3S)-3,7-DIAMINOHEPTANOIC+ACID'>B3K</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=5hi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hi1 OCA], [https://pdbe.org/5hi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hi1 RCSB], [https://www.ebi.ac.uk/pdbsum/5hi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hi1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG] | |||
<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 5hi1" style="background-color:#fffaf0;"></div> | ||
[[Category: Griffith | |||
[[Category: Horne | ==See Also== | ||
[[Category: Lengyel | *[[Protein G|Protein G]] | ||
[[Category: Tavenor | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus sp. 'group G']] | |||
[[Category: Griffith BD]] | |||
[[Category: Horne WS]] | |||
[[Category: Lengyel GA]] | |||
[[Category: Reinert ZE]] | |||
[[Category: Tavenor NA]] | |||
Latest revision as of 07:37, 9 August 2023
Backbone Modifications in the Protein GB1 Helix: Aib24, beta-3-Lys28, beta-3-Lys31, Aib35
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