ArticleBiomolecules2020
Structure of the Hydrophobic Core Determines the 3D Protein Structure-Verification by Single Mutation Proteins.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Engineering Biomimetic 3D Microenvironments for Extracellular Vesicle Programming Toward Clinical Translation.International journal of molecular sciences · 2026Review
- IscS Kinetics in Native Mass Spectrometry Buffers Reveal Key Physiochemical Properties that Influence Enzyme Activity.Journal of the American Society for Mass Spectrometry · 2026Article
- Deep-learning structure elucidation from single-mutant deep mutational scanning.Nature communications · 2025Article
- Chameleon sequences-Structural effects.PloS one · 2025Article
- Chameleon Sequences-Structural Effects in Proteins Characterized by Hydrophobicity Disorder.ACS omega · 2024Article
- Molecular Mechanisms Involved in the B Cell Growth and Clonogenic Activity of HIV-1 Matrix Protein p17 Variants.Viruses · 2024Article
- Structural studies of intrinsically disordered MLL-fusion protein AF9 in complex with peptidomimetic inhibitors.Protein science : a publication of the Protein Society · 2024Article
- Physical-Chemical Features Selection Reveals That Differences in Dipeptide Compositions Correlate Most with Protein-Protein Interactions.bioRxiv : the preprint server for biology · 2024Article
- Hydrophobicity-Based Force Field In Enzymes.ACS omega · 2024Article
- TIMED-Design: flexible and accessible protein sequence design with convolutional neural networks.Protein engineering, design & selection : PEDS · 2024Article
- Charting Peptide Shared Sequences Between 'Diabetes-Viruses' and Human Pancreatic Proteins, Their Structural and Autoimmune Implications.Bioinformatics and biology insights · 2024Article
- Cellular and epigenetic perspective of protein stability and its implications in the biological system.Epigenomics · 2024Review
- Structural and functional analyses of viral H2 protein of the vaccinia virus entry fusion complex.Journal of virology · 2023Article
- Molecular Docking and Molecular Dynamics Simulations in Related toTropical medicine and infectious disease · 2023Review
- The Role of Transmembrane Proteins in Plant Growth, Development, and Stress Responses.International journal of molecular sciences · 2022Review
- A second chance for protein targeting/folding: Ubiquitination and deubiquitination of nascent proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Review
- Lightweight ProteinUnet2 network for protein secondary structure prediction: a step towards proper evaluation.BMC bioinformatics · 2022Article
- On the Dependence of Prion and Amyloid Structure on the Folding Environment.International journal of molecular sciences · 2021Article
- Divergence Entropy-Based Evaluation of Hydrophobic Core in Aggressive and Resistant Forms of Transthyretin.Entropy (Basel, Switzerland) · 2021Article
- Recent Progress Using De Novo Design to Study Protein Structure, Design and Binding Interactions.Life (Basel, Switzerland) · 2021Review
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5 authors.
Funding
Abstract
Four de novo proteins differing in single mutation positions, with a chain length of 56 amino acids, represent diverse 3D structures: monomeric 3α and 4β + α folds. The reason for this diversity is seen in the different structure of the hydrophobic core as a result of synergy leading to the generation of a system in which the polypeptide chain as a whole participates. On the basis of the fuzzy oil drop model, where the structure of the hydrophobic core is expressed by means of the hydrophobic distribution function in the form of a 3D Gaussian distribution, it has been shown that the composition of the hydrophobic core in these two structural forms is different. In addition, the use of a model to determine the structure of the early intermediate in the folding process allows to indicate differences in the polypeptide chain geometry, which, combined with the construction of a common hydrophobic nucleus as an effect of specific synergy, may indicate the reason for the diversity of the folding process of the polypeptide chain. The results indicate the need to take into account the presence of an external force field originating from the water environment and that its active impact on the formation of a hydrophobic core whose participation in the stabilization of the tertiary structure is fundamental.
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