8t0i | pdb_00008t0i

Backbone Dialkylation in Peptide Hairpins: (R)-Ethylpropylglycine variant

spinqualitylabelsall models 8t0i Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8t0i is a 1 chain structure with sequence from Streptococcus sp. 'group G'. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: NH2, X6E Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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