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It has also been shown previously that \u03b22GPI can undergo a number of different post-translational modifications, altering its function and structure. It is unclear how the post translational modifications (PTMs) alter the progression through structures and if this alters the function of \u03b22GPI. To study this we have chosen to use molecular dynamics simulations, providing fine atomistic details on the transition between structures, which can then be compared to findings published in the literature for validation. This study aimed to identify the potential effects of PTMs on the structure of \u03b22GPI in-silico. Molecular simulations were carried out under standard physiological conditions (pH 7.4, 155 mM ionic strength, 1\u00a0bar pressure) for four models of \u03b22GPI. These were the wild type, plasmin clipped (with terminal 8 amino acids removed), deglycosylated (with all four glycans removed) and reduced (with the terminal disulfide bond removed between C288-C326). Three repeats of 100 ns were carried out for each model. Plasmin cleavage and reduction generated structures absent from the wild type (WT). Plasmin cleavage generated a more compact structure with altered movement in Domain I (residues 1 to 60), whilst reduction produced unique elongated structures. These corroborated already published findings. Interestingly no simulation showed \u03b22GPI circularise in these physiological simulations suggesting closing may not be an energetically favourable process. Molecular simulations of \u03b22GPI identified structures only available to specific post translationally modified variants, and failed to show re-circularisation. Molecular simulations of \u03b22GPI identified structures only available to specific post translationally modified variants, and failed to show re-circularisation.<\/jats:p>","DOI":"10.1038\/s41598-026-52707-0","type":"journal-article","created":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T10:55:35Z","timestamp":1779274535000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Molecular dynamics simulations of beta-2-glycoprotein 1 (\u03b22GPI) reveal that post-translational modifications facilitate novel structures"],"prefix":"10.1038","volume":"16","author":[{"given":"Christophe J.","family":"Lalaurie","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul A.","family":"Dalby","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"McDonnell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,5,20]]},"reference":[{"issue":"6","key":"52707_CR1","doi-asserted-by":"publisher","first-page":"556","DOI":"10.1016\/j.bbapap.2019.03.007","volume":"1867","author":"M Baerenfaenger","year":"2019","unstructured":"Baerenfaenger, M. & Meyer, B. 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