ReviewIntrinsically disordered proteins
The alphabet of intrinsic disorder: II. Various roles of glutamic acid in ordered and intrinsically disordered proteins.
Review in Intrinsically disordered proteins. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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72 citing papers in PubMed.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Phytochemical targeting of SASP2-mediated DNA protection to impair spore resilience in Bacillus cereus: A Computational Investigation.Molecular diversity · 2026Article
- Functional diversification across yeast lineages of the nucleus-vacuole junction forming protein Nvj1.bioRxiv : the preprint server for biology · 2026Article
- MBPBERT: A Large Language Model for Metal-Binding Peptide Discovery.Interdisciplinary sciences, computational life sciences · 2026Article
- Conjugates of Heme and Intrinsically Disordered Peptides toward the Development of Synthetic Artificial Oxygen Carriers.Bioconjugate chemistry · 2026Article
- Article
- Residue-level mapping of crowding effects on protein phase separation.Protein science : a publication of the Protein Society · 2026Article
- Integrative profiling of condensation-prone RNAs during early development.Cell genomics · 2026Article
- Various Ways to Be Negative: Biophysical Characterization of Polyanionic Biomolecules.The journal of physical chemistry. B · 2026Article
- Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- A deep learning method for predicting interactions for intrinsically disordered regions of proteins.bioRxiv : the preprint server for biology · 2025Article
- Functions of secretory calcium-binding phosphoproteins in dental mineralization.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2025Review
- Noncovalent Lasso Entanglements are Common in Experimentally Derived Intrinsically Disordered Protein Ensembles and Strongly Influenced by Protein Length and Charge.The journal of physical chemistry. B · 2025Article
- ASR gene family: a case of tandem-drive evolution.Frontiers in molecular biosciences · 2025Article
- Isoelectric point, net charge and amino acid analysis of experimentally validated therapeutic antibodies.In silico pharmacology · 2025Article
- Navigating the unstructured by evaluating alphafold's efficacy in predicting missing residues and structural disorder in proteins.PloS one · 2025Article
- Use of AI-methods over MD simulations in the sampling of conformational ensembles in IDPs.Frontiers in molecular biosciences · 2025Review
- Installation of an Indole on the BRCA1 Disordered Domain Using Triazine Chemistry.Biomolecules · 2024Article
- High-throughput Selection of Human de novo-emerged sORFs with High Folding Potential.Genome biology and evolution · 2024Article
- Protein structure-function continuum model: Emerging nexuses between specificity, evolution, and structure.Protein science : a publication of the Protein Society · 2024Review
12 more citing papers are in PubMed but not listed here.
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Abstract
The ability of a protein to fold into unique functional state or to stay intrinsically disordered is encoded in its amino acid sequence. Both ordered and intrinsically disordered proteins (IDPs) are natural polypeptides that use the same arsenal of 20 proteinogenic amino acid residues as their major building blocks. The exceptional structural plasticity of IDPs, their capability to exist as heterogeneous structural ensembles and their wide array of important disorder-based biological functions that complements functional repertoire of ordered proteins are all rooted within the peculiar differential usage of these building blocks by ordered proteins and IDPs. In fact, some residues (so-called disorder-promoting residues) are noticeably more common in IDPs than in sequences of ordered proteins, which, in their turn, are enriched in several order-promoting residues. Furthermore, residues can be arranged according to their "disorder promoting potencies," which are evaluated based on the relative abundances of various amino acids in ordered and disordered proteins. This review continues a series of publications on the roles of different amino acids in defining the phenomenon of protein intrinsic disorder and concerns glutamic acid, which is the second most disorder-promoting residue.
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