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. 2021 May 3;118(19):e2024117118. doi: 10.1073/pnas.2024117118

Fig. 1.

Fig. 1.

Design and physical characterization of synthetic Gal3 constructs with tunable valency. (A) Library of 2- to 6-stranded parallel, α-helical coiled-coil peptide scaffolds for the assembly of defined oligomers from monomeric Gal3 fusion proteins (i.e., Monomer). (B) Schematic presentation of Monomer and synthetic Gal3 oligomers (i.e., Dimer-Hexamer). (C) Schematic presentation of Monomer-Hexamer top and bottom views. (D) Distribution of hydrodynamic size demonstrated via SEC. (E) Average hydrodynamic diameter determined via DLS. For E, histograms are a single representative experiment from three replicate size measurements per construct. Protein Data Bank (PDB) ID: 4DMD (2-stranded coiled-coil); 2O7H (3-stranded coiled-coil); 1GCL (4-stranded coiled-coil); 4PN8 (5-stranded coiled-coil); 3R3K (6-stranded coiled-coil); 2B3P (sfGFP); 5NF7 (Gal3 carbohydrate-recognition domain).