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However, recent NMR studies have revealed unintended structural and dynamic heterogeneity in an ultra-stable computationally designed miniprotein, EHEE_rd2_0005, at elevated temperatures and long timescales. As de novo protein design continues to expand, robust methods are needed to thoroughly characterize computationally generated proteins and identify such behavior prior to therapeutic application. Here, we benchmark replica exchange molecular dynamics (REMD) simulations against conventional molecular dynamics (MD) for predicting residue-level structure and dynamics in EHEE_rd2_0005 and additional model miniproteins previously characterized by NMR. We find that both REMD and standard high temperature MD produce conformational dynamics that are in strong agreement with experimental HDX-NMR measurements. Furthermore, REMD enables the development of an accurate predictive model for miniprotein HDX and shows that miniproteins of comparable stability are predictive of each other’s dynamics. Additionally, REMD and high temperature MD successfully sample the rotation between two conformations of a tryptophan sidechain in intermediate exchange, a dynamic process involving residue W35 of EHEE_rd2_0005 not previously observed in simulations. Together, these results establish REMD, as well as MD at elevated temperature, as effective approaches for probing long-timescale dynamics in miniproteins that may otherwise go unnoticed without extensive NMR experimentation. As the use of computational protein design continues to expand, REMD should be considered a tool for characterizing the structure and dynamics of de novo miniproteins therapeutics.</p>"},{"label":"Digital Identifier","value":"b2026-Levine"},{"label":"Digital Object Identifier (DOI)","value":"https://doi.org/10.14418/mw7ibtqf"},{"label":"Digital Origin","value":["born digital"]},{"label":"Discipline","value":["Biology"]},{"label":"Date","value":"April 15, 2026"},{"label":"EDTF Date","value":"D:00 M:00 Y:2026"},{"label":"File Format","value":["application/pdf"]},{"label":"Genre","value":["theses"]},{"label":"Group","value":["Theses & Dissertations"]},{"label":"Held By","value":"Wesleyan University Library, Wesleyan University, Middletown, CT, USA"},{"label":"Language","value":["English"]},{"label":"Repository","value":["University Archives"]},{"label":"Rights","value":["In Copyright"]},{"label":"Thesis Advisor(s)","value":["Smith, Colin 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