9ola

Backbone-modified parallel beta hairpin (PBH): N-alpha-amino Tyrosine at position 15

spinqualitylabelsall models 9ola Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ola is a 2 chain structure with sequence from Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 10 models Ligands: 4G6, A1CCQ, ACE, DPR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Peptide backbone N-amination has emerged as a useful strategy to stabilize antiparallel beta-sheet structure. Here, we used circular dichroism and NMR to evaluate the impact of amide-to-hydrazide substitution on the folded population of a parallel beta-hairpin model. Outer-edge N-amination was well tolerated and resulted in enhanced stability relative to N-methylation. High-resolution NMR structures confirmed that the alpha-hydrazino acid residues adopt canonical parallel beta-strand torsions that are compatible with the formation of intraresidue C6 hydrogen bonds involving the hydrazide NH(2) group. Impact of Strand Edge N-Amination on the Stability of a Parallel beta-Hairpin Fold.,Starnes SK, Horne WS, Del Valle JR J Org Chem. 2025 Nov 20. doi: 10.1021/acs.joc.5c02479. PMID:41264875 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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