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Structural Water Stabilizes Protein Motifs in Liquid Protein Phase: The Folding Mechanism of Short ß-Sheets Coupled to Phase Transition.
Papp, Dóra; Szigyártó, Imola Csilla; Nordén, Bengt; Perczel, András; Beke-Somfai, Tamás.
Afiliación
  • Papp D; Laboratory of Structural Chemistry and Biology, MTA ELTE Protein Modelling Research Group, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, H-1117 Budapest, Hungary.
  • Szigyártó IC; MTA-SZTE Lendület Computational Reaction Dynamics Research Group, Interdisciplinary Excellence Centre, Department of Physical Chemistry and Materials Science, Institute of Chemistry, University of Szeged, Rerrich Béla tér 1, H-6720 Szeged, Hungary.
  • Nordén B; Biomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117 Budapest, Hungary.
  • Perczel A; Department of Chemical and Biological Engineering, Physical Chemistry, Chalmers University of Technology, SE-412 96 Göteborg, Sweden.
  • Beke-Somfai T; Laboratory of Structural Chemistry and Biology, MTA ELTE Protein Modelling Research Group, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, H-1117 Budapest, Hungary.
Int J Mol Sci ; 22(16)2021 Aug 10.
Article en En | MEDLINE | ID: mdl-34445303
Macromolecular associates, such as membraneless organelles or lipid-protein assemblies, provide a hydrophobic environment, i.e., a liquid protein phase (LP), where folding preferences can be drastically altered. LP as well as the associated phase change from water (W) is an intriguing phenomenon related to numerous biological processes and also possesses potential in nanotechnological applications. However, the energetic effects of a hydrophobic yet water-containing environment on protein folding are poorly understood. Here, we focus on small ß-sheets, the key motifs of proteins, undergoing structural changes in liquid-liquid phase separation (LLPS) and also model the mechanism of energy-coupled unfolding, e.g., in proteases, during W → LP transition. Due to the importance of the accurate description for hydrogen bonding patterns, the employed models were studied by using quantum mechanical calculations. The results demonstrate that unfolding is energetically less favored in LP by ~0.3-0.5 kcal·mol-1 per residue in which the difference further increased by the presence of explicit structural water molecules, where the folded state was preferred by ~1.2-2.3 kcal·mol-1 per residue relative to that in W. Energetics at the LP/W interfaces was also addressed by theoretical isodesmic reactions. While the models predict folded state preference in LP, the unfolding from LP to W renders the process highly favorable since the unfolded end state has >1 kcal·mol-1 per residue excess stabilization.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Agua / Transición de Fase / Conformación Proteica en Lámina beta Tipo de estudio: Prognostic_studies Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Suiza
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Agua / Transición de Fase / Conformación Proteica en Lámina beta Tipo de estudio: Prognostic_studies Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Suiza