ArticlePLoS computational biology2011
Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation.
Article in PLoS computational biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Amyloid fibril polymorphism: Structural mechanisms of assembly and the links to disease.Current opinion in structural biology · 2026Review
- The Stability and Digestive Characteristics of Soybean Protein Fibril/κ-Carrageenan Composite Gels for Riboflavin Encapsulation.Foods (Basel, Switzerland) · 2026Article
- Protein fibering combined with a composite network strategy to enhance the soybean protein-sodium alginate hydrogel.Current research in food science · 2026Article
- Interactions with tau's microtubule-binding repeats modulate amyloid-β aggregation and toxicity.Nature chemical biology · 2025Article
- Complexation with Ionic Polysaccharides Mitigates pH-Dependent Degradation of Soy Protein Fibril Structure and Functionality.Journal of agricultural and food chemistry · 2025Article
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- Predictive Model Building for Aggregation Kinetics Based on Molecular Dynamics Simulations of an Antibody Fragment.Molecular pharmaceutics · 2024Article
- Prediction of the most deleterious non-synonymous SNPs in the human IL1B gene: evidence from bioinformatics analyses.BMC genomic data · 2024Article
- β-Bracelets: Macrocyclic Cross-β Epitope Mimics Based on a Tau Conformational Strain.Journal of the American Chemical Society · 2023Article
- Mesalazine Inhibits Amyloid Formation and Destabilizes Pre-formed Amyloid Fibrils in the Human Insulin.Journal of fluorescence · 2023Article
- Investigating the Effects of NaCl on the Formation of AFs from Gluten in Cooked Wheat Noodles.International journal of molecular sciences · 2023Article
- Disassembly of Amyloid Fibril with Infrared Free Electron Laser.International journal of molecular sciences · 2023Review
- Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies.International journal of molecular sciences · 2023Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
- A coarse-grained mechanical model for folding and unfolding of tropoelastin with possible mutations.Acta biomaterialia · 2021Article
- Zinc Binding to NAP-Type Neuroprotective Peptides: Nuclear Magnetic Resonance Studies and Molecular Modeling.Pharmaceuticals (Basel, Switzerland) · 2021Article
- A quantitative calcium phosphate nanocluster model of the casein micelle: the average size, size distribution and surface properties.European biophysics journal : EBJ · 2021Article
- Charge Regulation during Amyloid Formation of α-Synuclein.Journal of the American Chemical Society · 2021Article
- Thermodynamic and Evolutionary Coupling between the Native and Amyloid State of Globular Proteins.Cell reports · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Identifying the forces that drive proteins to misfold and aggregate, rather than to fold into their functional states, is fundamental to our understanding of living systems and to our ability to combat protein deposition disorders such as Alzheimer's disease and the spongiform encephalopathies. We report here the finding that the balance between hydrophobic and hydrogen bonding interactions is different for proteins in the processes of folding to their native states and misfolding to the alternative amyloid structures. We find that the minima of the protein free energy landscape for folding and misfolding tend to be respectively dominated by hydrophobic and by hydrogen bonding interactions. These results characterise the nature of the interactions that determine the competition between folding and misfolding of proteins by revealing that the stability of native proteins is primarily determined by hydrophobic interactions between side-chains, while the stability of amyloid fibrils depends more on backbone intermolecular hydrogen bonding interactions.
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