ArticleInternational journal of molecular sciences2016
Structural Interface Forms and Their Involvement in Stabilization of Multidomain Proteins or Protein Complexes.
Article in International journal of molecular sciences, 2016. 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.
- Activity of Serpins in Context to Hydrophobic Interaction.Biomolecules · 2025Article
- Three scenarios for amyloid transformation in the context of the funnel model.Computational and structural biotechnology journal · 2025Article
- Protein folding: Funnel model revised.Computational and structural biotechnology journal · 2024Article
- Domain swapping: a mathematical model for quantitative assessment of structural effects.FEBS open bio · 2024Article
- 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
- 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 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
- 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
- Solubility and Aggregation of Selected Proteins Interpreted on the Basis of Hydrophobicity Distribution.International journal of molecular sciences · 2021Article
- 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
- Towards the design of anti-amyloid short peptide helices.Bioinformation · 2018Article
- Propagation of Fibrillar Structural Forms in Proteins Stopped by Naturally Occurring Short Polypeptide Chain Fragments.Pharmaceuticals (Basel, Switzerland) · 2017Article
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6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presented analysis concerns the inter-domain and inter-protein interface in protein complexes. We propose extending the traditional understanding of the protein domain as a function of local compactness with an additional criterion which refers to the presence of a well-defined hydrophobic core. Interface areas in selected homodimers vary with respect to their contribution to share as well as individual (domain-specific) hydrophobic cores. The basic definition of a protein domain, i.e., a structural unit characterized by tighter packing than its immediate environment, is extended in order to acknowledge the role of a structured hydrophobic core, which includes the interface area. The hydrophobic properties of interfaces vary depending on the status of interacting domains-In this context we can distinguish: (1) Shared hydrophobic cores (spanning the whole dimer); (2) Individual hydrophobic cores present in each monomer irrespective of whether the dimer contains a shared core. Analysis of interfaces in dystrophin and utrophin indicates the presence of an additional quasi-domain with a prominent hydrophobic core, consisting of fragments contributed by both monomers. In addition, we have also attempted to determine the relationship between the type of interface (as categorized above) and the biological function of each complex. This analysis is entirely based on the fuzzy oil drop model.
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