ArticleInternational journal of molecular sciences2021
Structural Water Stabilizes Protein Motifs in Liquid Protein Phase: The Folding Mechanism of Short β-Sheets Coupled to Phase Transition.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 6 citations in OpenAlex.
- A Deep-Learning Neural Network Potential Accelerated First-Principles Study on the Structural Changes Modulated by Methylation and Solvation in 27 Protonated Tripeptides.The journal of physical chemistry. A · 2025Article
- Membrane-Peptide Interactions: From Basics to Current Applications 2.0.International journal of molecular sciences · 2023Article
- On the Dependence of Prion and Amyloid Structure on the Folding Environment.International journal of molecular sciences · 2021Article
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5 authors at 3 institutions in 2 countries.
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Abstract
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 β-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
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