ArticleMembranes2021
Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins.
Article in Membranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 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
- Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone.BMC bioinformatics · 2023Article
- 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
- The Possible Mechanism of Amyloid Transformation Based on the Geometrical Parameters of Early-Stage Intermediate in Silico Model for Protein Folding.International journal of molecular sciences · 2022Article
- Connexins and Pannexins-Similarities and Differences According to the FOD-M Model.Biomedicines · 2022Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The natural environment of proteins is the polar aquatic environment and the hydrophobic (amphipathic) environment of the membrane. The fuzzy oil drop model (FOD) used to characterize water-soluble proteins, as well as its modified version FOD-M, enables a mathematical description of the presence and influence of diverse environments on protein structure. The present work characterized the structures of membrane proteins, including those that act as channels, and a water-soluble protein for contrast. The purpose of the analysis was to verify the possibility that an external force field can be used in the simulation of the protein-folding process, taking into account the diverse nature of the environment that guarantees a structure showing biological activity.
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Registered trials
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