ArticleInternational journal of molecular sciences2018
Physical Background of the Disordered Nature of "Mutual Synergetic Folding" Proteins.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Molecular Dynamics Simulation as a Tool to Identify Mutual Synergistic Folding Proteins.International journal of molecular sciences · 2023Article
- Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins.International journal of molecular sciences · 2021Article
- Experimentally Determined Long Intrinsically Disordered Protein Regions Are Now Abundant in the Protein Data Bank.International journal of molecular sciences · 2020Article
- Macromolecular Interactions of Disordered Proteins.International journal of molecular sciences · 2020Article
- Sequence and Structure Properties Uncover the Natural Classification of Protein Complexes Formed by Intrinsically Disordered Proteins via Mutual Synergistic Folding.International journal of molecular sciences · 2019Article
- Analysis of Heterodimeric "Mutual Synergistic Folding"-Complexes.International journal of molecular sciences · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Intrinsically disordered proteins (IDPs) lack a well-defined 3D structure. Their disordered nature enables them to interact with several other proteins and to fulfil their vital biological roles, in most cases after coupled folding and binding. In this paper, we analyze IDPs involved in a new mechanism, mutual synergistic folding (MSF). These proteins define a new subset of IDPs. Recently we collected information on these complexes and created the Mutual Folding Induced by Binding (MFIB) database. These protein complexes exhibit considerable structural variation, and almost half of them are homodimers, but there is a significant amount of heterodimers and various kinds of oligomers. In order to understand the basic background of the disordered character of the monomers found in MSF complexes, the simplest part of the MFIB database, the homodimers are analyzed here. We conclude that MFIB homodimeric proteins have a larger solvent-accessible main-chain surface area on the contact surface of the subunits, when compared to globular homodimeric proteins. The main driving force of the dimerization is the mutual shielding of the water-accessible backbones and the formation of extra intermolecular interactions.
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