8t0g: Difference between revisions

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'''Unreleased structure'''


The entry 8t0g is ON HOLD  until Paper Publication
==Backbone Dialkylation in Peptide Hairpins: Natural Backbone Prototype==
<StructureSection load='8t0g' size='340' side='right'caption='[[8t0g]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8t0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8T0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8T0G FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=8t0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8t0g OCA], [https://pdbe.org/8t0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8t0g RCSB], [https://www.ebi.ac.uk/pdbsum/8t0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8t0g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Strategic incorporation of achiral C(alpha,alpha)-dialkylated amino acids with bulky substituents into peptides can be used to promote extended strand conformations and inhibit protein-protein interactions associated with amyloid formation. In this work, we evaluate the thermodynamic impact of chiral C(alpha,alpha) monomers on folding preferences in such systems through introduction of a series of C(alpha)-methylated and C(alpha)-ethylated residues into a beta-hairpin host sequence. Depending on stereochemical configuration of the artificial monomer and potential for additional hydrophobic packing, a C(alpha)-ethyl-C(alpha)-propyl glycine residue can provide similar or enhanced folded stability relative to an achiral C(alpha,alpha)-diethyl analogue.


Authors: Heath, S.L., Horne, W.S., Lengyel, G.A.
Effects of chirality and side chain length in C(alpha,alpha)-dialkylated residues on beta-hairpin peptide folded structure and stability.,Heath SL, Horne WS, Lengyel GA Org Biomol Chem. 2023 Aug 9;21(31):6320-6324. doi: 10.1039/d3ob00963g. PMID:37503895<ref>PMID:37503895</ref>


Description: Backbone Dialkylation in Peptide Hairpins: Natural Backbone Prototype
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Horne, W.S]]
<div class="pdbe-citations 8t0g" style="background-color:#fffaf0;"></div>
[[Category: Heath, S.L]]
== References ==
[[Category: Lengyel, G.A]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus sp. 'group G']]
[[Category: Heath SL]]
[[Category: Horne WS]]
[[Category: Lengyel GA]]
Retrieved from "https://proteopedia.org/8t0g"