8t0h: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8t0h]] 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=8T0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8T0H FirstGlance]. <br> | <table><tr><td colspan='2'>[[8t0h]] 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=8T0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8T0H 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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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>, <scene name='pdbligand=X60:2-ethyl- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=X60:(2~{S})-2-azanyl-2-ethyl-pentanoic+acid'>X60</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=8t0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8t0h OCA], [https://pdbe.org/8t0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8t0h RCSB], [https://www.ebi.ac.uk/pdbsum/8t0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8t0h 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=8t0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8t0h OCA], [https://pdbe.org/8t0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8t0h RCSB], [https://www.ebi.ac.uk/pdbsum/8t0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8t0h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 12:56, 17 October 2024
Backbone Dialkylation in Peptide Hairpins: (S)-Ethylpropylglycine variantBackbone Dialkylation in Peptide Hairpins: (S)-Ethylpropylglycine variant
Structural highlights
Publication Abstract from PubMedStrategic 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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