ArticleInternational journal of molecular sciences2021
Model of Environmental Membrane Field for Transmembrane Proteins.
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 15 papers.
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Who cites it
15 citing papers in PubMed.
- Chameleon sequences-Structural effects.PloS one · 2025Article
- Article
- Hydrophobicity-Based Force Field In Enzymes.ACS omega · 2024Article
- Model of the external force field for the protein folding process-the role of prefoldin.Frontiers in chemistry · 2024Article
- Role of environmental specificity in CASP results.BMC bioinformatics · 2023Article
- Main Factors Shaping Amino Acid Usage Across Evolution.Journal of molecular evolution · 2023Review
- Protein Is an Intelligent Micelle.Entropy (Basel, Switzerland) · 2023Article
- Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid.Biomedicines · 2023Article
- Engagement of intrinsic disordered proteins in protein-protein interaction.Frontiers in molecular biosciences · 2023Article
- The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins.Membranes · 2022Article
- Connexins and Pannexins-Similarities and Differences According to the FOD-M Model.Biomedicines · 2022Article
- Article
- Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins.Membranes · 2021Article
- In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model.International journal of molecular sciences · 2021Article
- The Functional Significance of Hydrophobic Residue Distribution in Bacterial Beta-Barrel Transmembrane Proteins.Membranes · 2021Article
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Authors and funding
5 authors.
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Abstract
The water environment determines the activity of biological processes. The role of such an environment interpreted in the form of an external field expressed by the 3D Gaussian distribution in the fuzzy oil drop model directs the folding process towards the generation of a centrally located hydrophobic core with the simultaneous exposure of polar residues on the surface. In addition to proteins soluble in the water environment, there is a significant group of membrane proteins that act as receptors or channels, including ion channels in particular. The change of the polar (water) environment into a highly hydrophobic (membrane) environment is quite radical, resulting in a different hydrophobicity distribution within the membrane protein. Modification of the notation of the force field expressing the presence of the hydrophobic environment has been proposed in this work. A modified fuzzy oil drop model with its adaptation to membrane proteins was used to interpret the structure of membrane proteins-mechanosensitive channel. The modified model was also used to describe the so-called negative cases-i.e., for water-soluble proteins with a clear distribution consistent with the fuzzy oil drop model.
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