ArticleJournal of molecular modeling2017
Is the hydrophobic core a universal structural element in proteins?
Article in Journal of molecular modeling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Engineering Biomimetic 3D Microenvironments for Extracellular Vesicle Programming Toward Clinical Translation.International journal of molecular sciences · 2026Review
- Decoding the Post-translational Modification Crosstalk: Functional Implications of Phosphorylation, Acetylation, and Methylation.The journal of physical chemistry. B · 2026Article
- Optimized Multi-Epitope Norovirus Vaccines Induce Robust Humoral and Cellular Responses in Mice.Vaccines · 2025Article
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- Recent advances in extracellular vesicles for therapeutic cargo delivery.Experimental & molecular medicine · 2024Review
- Ordered-domain unfolding of thermophilic isolated β subunit ATP synthase.Protein science : a publication of the Protein Society · 2023Article
- Conformational changes in the catalytic region are responsible for heat-induced activation of hyperthermophilic homoserine dehydrogenase.Communications biology · 2022Article
- The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response.Archives of toxicology · 2021Review
- Downhill, Ultrafast and Fast Folding Proteins Revised.International journal of molecular sciences · 2020Article
- The Structure of Amyloid Versus the Structure of Globular Proteins.International journal of molecular sciences · 2020Article
- Structure of the Hydrophobic Core Determines the 3D Protein Structure-Verification by Single Mutation Proteins.Biomolecules · 2020Article
- The Amyloid as a Ribbon-Like Micelle in Contrast to Spherical Micelles Represented by Globular Proteins.Molecules (Basel, Switzerland) · 2019Review
- Different Synergy in Amyloids and Biologically Active Forms of Proteins.International journal of molecular sciences · 2019Article
- Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model.International journal of molecular sciences · 2018Article
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Authors and funding
5 authors.
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Abstract
The hydrophobic core, when subjected to analysis based on the fuzzy oil drop model, appears to be a universal structural component of proteins irrespective of their secondary, supersecondary, and tertiary conformations. A study has been performed on a set of nonhomologous proteins representing a variety of CATH categories. The presence of a well-ordered hydrophobic core has been confirmed in each case, regardless of the protein's biological function, chain length or source organism. In light of fuzzy oil drop (FOD) analysis, various supersecondary forms seem to share a common structural factor in the form of a hydrophobic core, emerging either as part of the whole protein or a specific domain. The variable status of individual folds with respect to the FOD model reflects their propensity for conformational changes, frequently associated with biological function. Such flexibility is expressed as variable stability of the hydrophobic core, along with specific encoding of potential conformational changes which depend on the properties of helices and β-folds.
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