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. 2024 Jan 24;25(3):1436. doi: 10.3390/ijms25031436

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© 2024 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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(A–C). Effect of the variant c.1259C>A, p.Thr420Lys on protein dynamics and stability by DynaMut. Wild-type (A) and mutant residues (B) are colored in light-green, showing the difference between interactions (along with surrounding residues) involved in any type of interactions. (C) Effect of vibrational entropy changes induced by aa variation due to c.1259C>A variant. The blue area represents a rigidification of the structure. (D–F) The effect of the variant c.937G>T, p.Asp313Tyr (D313Y) on protein dynamics and stability by DynaMut, Wild-type (D) and mutant residues (E) are colored in light-green, showing the difference between interactions and surrounding residues) involved in any type of interactions. (F) Effect of vibrational entropy changes induced by aa variation, due to the c.937G>T variant.