8T0I
Backbone Dialkylation in Peptide Hairpins: (R)-Ethylpropylglycine variant
Summary for 8T0I
| Entry DOI | 10.2210/pdb8t0i/pdb |
| NMR Information | BMRB: 31091 |
| Descriptor | Immunoglobulin G-binding protein G (1 entity in total) |
| Functional Keywords | hairpin, peptidomimetic, backbone modification, de novo protein |
| Biological source | Streptococcus sp. group G |
| Total number of polymer chains | 1 |
| Total formula weight | 1883.07 |
| Authors | Heath, S.L.,Horne, W.S.,Lengyel, G.A. (deposition date: 2023-06-01, release date: 2023-08-16, Last modification date: 2023-11-15) |
| Primary citation | 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. Org.Biomol.Chem., 21:6320-6324, 2023 Cited by PubMed Abstract: Strategic incorporation of achiral C-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 monomers on folding preferences in such systems through introduction of a series of C-methylated and C-ethylated residues into a β-hairpin host sequence. Depending on stereochemical configuration of the artificial monomer and potential for additional hydrophobic packing, a C-ethyl-C-propyl glycine residue can provide similar or enhanced folded stability relative to an achiral C-diethyl analogue. PubMed: 37503895DOI: 10.1039/d3ob00963g PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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