9bb2

Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 20 and 24

spinqualitylabelsall models 9bb2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9bb2 is a 1 chain structure with sequence from Finegoldia magna. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: B3D, B3X, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAB_FINMA Binds serum albumin. Publication Abstract from PubMed Targeted protein backbone modification can recreate tertiary structures reminiscent of folds found in nature on artificial scaffolds with improved biostability. Incorporation of altered monomers in such entities is typically limited to sites distant from the hydrophobic core to avoid potential disruptions to folding. This is limiting, as it is advantageous in some applications to incorporate artificial connectivity at buried sites. Here, we report an examination of protein backbone modification targeted specifically to hydrophobic core positions and its impacts on tertiary folded structure and fold stability. Different artificial monomer types are placed at core, core-flanking, or solvent-exposed positions in a compact three-helix protein. Effects on structure and folding energetics are assessed by NMR spectroscopy and biophysical methods. Results show that artificial residues can be well accommodated in the hydrophobic core of a defined tertiary fold, with effects on stability only modestly larger than identical changes at solvent-exposed sites. Collectively, these results provide new insights into folding behavior of protein-like artificial chains as well as strategies for the design of such molecules. Backbone Modification in a Protein Hydrophobic Core.,Lin Y, Horne WS Chemistry. 2024 May 16:e202401890. doi: 10.1002/chem.202401890. PMID:38753977 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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