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[Preprint]. 2023 Apr 25:2023.03.13.532222. Originally published 2023 Mar 14. [Version 2] doi: 10.1101/2023.03.13.532222

Figure 2. HT6-Ub constructs with longer linkers are larger in size and more extended in overall conformation.

Figure 2.

(A) Library of HT6-Ub constructs with different linkers with a cartoon representation of the spider-like HT6-Ub geometric architecture. (B) Experimental X-ray scattering curves (black) for designed HT6-(PA)x-Ub constructs overlaid with scattering curve predicted (red) from single best structure (shown) derived from SASSIE conformational ensembles. Hydrophobic patch residues L8, I44, and V70 are represented as yellow spheres. (C,D) P(r) profiles from SAXS experiments on HT6-Ub ligands of different linker lengths. (E) Radius of gyration (Rg) as determined from Guinier fits to SAXS experiments for HT6-Ub constructs (closed circles: GS series and open circles: PA series) as a function of linker length (# of amino acids). Black dotted lines represent simple linear regression of each data set.