The DOI matches its Crossref record; 86 of the 86 references it cites were found in a registry or an index.
Fuzzy Complexes: A More Stochastic View of Protein Function
Abstract
Intrinsically disordered proteins (IDPs) are widespread in eukaryotic proteomes and challenge the classical structure-function paradigm that equates a folded 3-D structure with protein function. However, IDPs often function by molecular recognition, in which they bind a partner molecule and undergo "induced folding" or "disorder-to-order transition" upon binding, which apparently suggests that in a functional context IDPs become ordered. Whereas this observation would restore the "prestige" of the classical structure-function paradigm, a closer inspection of the complexes of IDPs reveals that they do not always become fully ordered, but preserve functionally significant disorder in the complex with their binding partner(s). This phenomenon, which we termed "fuzziness", is the ultimate extension of structural disorder to the functional native state of proteins. In this introductory chapter, we outline the most important aspects of fuzziness, such as its structural categories, molecular mechanisms of function it mediates and the biological processes, in which it plays a distinguished role. As confirmed by all the other chapters of the book, we will show that new cases of fuzziness pop up at an accelerating pace, underscoring that this phenomenon presents a widespread novel paradigm of protein structure and function.
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“Some IDPs/IDRs may remain unfolded and dynamic even in the bound state [19–23], creating fuzzy complexes (Fig. 1) [24, 25].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [25]
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AlphaFold and Implications for Intrinsically Disordered Proteins
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Unusual biophysics of intrinsically disordered proteins
Uversky, V. N. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.008 · Cited by 581
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Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour
Fusco, G., Simone, A. D., Gopinath, T., Vostrikov, V. V., Vendruscolo, M., Dobson, C. M., & Veglia, G. (2014) · Nature Communications · doi:10.1038/ncomms4827 · Cited by 493
Metadata
- Authors
- Fuxreiter, M., & Tompa, P.
- Venue
- Advances in Experimental Medicine and Biology
- Publisher
- Springer US
- Published
- 2012
- Volume
- 725
- Pages
- 1-14
- ISSN
- 0065-2598 (ISSN-L)
- OpenAlex
- W2243182195
- Cited by
- 240
- References
- 86
- Citations by year
- 2026: 9 · 2025: 10 · 2024: 24 · 2023: 7 · 2022: 12 · 2021: 20 · 2020: 19 · 2019: 18 · 2018: 20 · 2017: 17 · 2016: 19 · 2015: 23 · 2014: 13 · 2013: 24 · 2012: 5
- FWCI
- 35.58
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Advances in experimental medicine and biology (publishedVersion)
- PubMed (publishedVersion)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- intrinsically disordered proteins, fuzziness, protein complexes, induced folding, disorder-to-order transition, protein function, structure-function relationship, molecular recognition, protein-protein interaction
- MeSH terms
- Animals, Humans, Models, Molecular, Protein Binding, Proteins, Protein Structure, Tertiary, Protein Folding
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