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. 2023 Jun 1;32(6):e4653. doi: 10.1002/pro.4653

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© 2023 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.

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Experimental characterization of the designs. (a) The superimposed structures of the design predicted by AlphaFold2 (colored) versus the original (gray) structure. (b) The SEC‐MALS measurements indicated that protein G_1 and top7_10 appear in monomeric and dimeric forms, whereas 4H_1 appears purely as a monomer. The expected Molecular Weight (MW) of the designs was 7.7 kDa for protein G_1, 11.7 kDa for protein top7_10, and 11.2 kDa for protein 4H_1. (c) The CD spectra of the designs showed that the designs were folded. (d) Temperature melting curves per design. Full experimental characterization of all folded designs can be found in Figure S9.