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. 2024 Mar 14;15:2202. doi: 10.1038/s41467-024-46295-8

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — A Amino acid analysis of DT-preF. Samples were acid-hydrolyzed and analyzed for amino acid content using a Concise AminoSep Beckman Style Na+ column and a Hitachi analytical HPLC. Table (top) with calculated Dityrosine (Di-Tyr) bonds in the DT-preF sample utilizing the experimentally determined percentage recovery and quantification information. Chromatogram (bottom left) indicating the detection of the dityrosine peak in the DT-preF sample. Table (bottom right) indicating list of amino acids detected in the analysis with the respective peak attributes/quantification. Amino acid analysis was performed a single time. B Chromatograms of uncrosslinked F protein containing the DT mutations, preF^C (top left) and DT-preF (bottom left) showing fluorescence (green) and UV (gray) traces at increasing retention times (min) following separation using analytical size exclusion chromatography under reducing and denaturing conditions. Chromatogram showing fluorescence (green) and UV (gray) traces of DT-preF (top right) and its corresponding SDS-PAGE analysis gel (bottom right) indicating separation of the dimer/trimer peak from the monomer peak, as indicated. This separation between multimers and monomers observed on SDS-PAGE analysis gels has been observed and reproduced in >3 independent experiments.