ArticleEntropy (Basel, Switzerland)2019
Entropy and Information within Intrinsically Disordered Protein Regions.
Article in Entropy (Basel, Switzerland), 2019. 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.
- AI-driven multiscale virtual plant cell modeling: from molecular mechanisms to tissue functions.Planta · 2026Review
- Article
- Comprehensive Analysis of the GXXXG Motif Reveals Structural Context-Dependent Diversity and Composition Across Proteins.International journal of molecular sciences · 2025Article
- Disordered Regions of Condensate-promoting Proteins Have Distinct Molecular Signatures Associated with Cellular Function.Journal of molecular biology · 2025Article
- Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Leaderless secretory proteins of the neurodegenerative diseases via TNTs: a structure-function perspective.Frontiers in molecular neuroscience · 2023Review
- The difficulty of aligning intrinsically disordered protein sequences as assessed by conservation and phylogeny.PloS one · 2023Article
- Chemical tools for study and modulation of biomolecular phase transitions.Chemical science · 2022Review
- Information Theory for Biological Sequence Classification: A Novel Feature Extraction Technique Based on Tsallis Entropy.Entropy (Basel, Switzerland) · 2022Article
- Discovering molecular features of intrinsically disordered regions by using evolution for contrastive learning.PLoS computational biology · 2022Article
- Arrow of Time, Entropy, and Protein Folding: Holistic View on Biochirality.International journal of molecular sciences · 2022Review
- A functionally divergent intrinsically disordered region underlying the conservation of stochastic signaling.PLoS genetics · 2021Article
- Thermodynamic Compensation in Peptides Following Liquid-Liquid Phase Separation.The journal of physical chemistry. B · 2021Article
- A weakened interface in the P182L variant of HSP27 associated with severe Charcot-Marie-Tooth neuropathy causes aberrant binding to interacting proteins.The EMBO journal · 2021Article
- Uncovering patterns of the evolution of genomic sequence entropy and complexity.Molecular genetics and genomics : MGG · 2021Article
- Physical Chemistry of the Protein Backbone: Enabling the Mechanisms of Intrinsic Protein Disorder.The journal of physical chemistry. B · 2020Review
- Conditional Disorder in Small Heat-shock Proteins.Journal of molecular biology · 2020Article
- Mutually exclusive locales for N-linked glycans and disorder in human glycoproteins.Scientific reports · 2020Article
- A model ofPeerJ · 2020Article
- Dissecting the Energetics of Intrinsically Disordered Proteins via a Hybrid Experimental and Computational Approach.The journal of physical chemistry. B · 2019Article
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4 authors.
Funding
Abstract
Bioinformatics and biophysical studies of intrinsically disordered proteins and regions (IDRs) note the high entropy at individual sequence positions and in conformations sampled in solution. This prevents application of the canonical sequence-structure-function paradigm to IDRs and motivates the development of new methods to extract information from IDR sequences. We argue that the information in IDR sequences cannot be fully revealed through positional conservation, which largely measures stable structural contacts and interaction motifs. Instead, considerations of evolutionary conservation of molecular features can reveal the full extent of information in IDRs. Experimental quantification of the large conformational entropy of IDRs is challenging but can be approximated through the extent of conformational sampling measured by a combination of NMR spectroscopy and lower-resolution structural biology techniques, which can be further interpreted with simulations. Conformational entropy and other biophysical features can be modulated by post-translational modifications that provide functional advantages to IDRs by tuning their energy landscapes and enabling a variety of functional interactions and modes of regulation. The diverse mosaic of functional states of IDRs and their conformational features within complexes demands novel metrics of information, which will reflect the complicated sequence-conformational ensemble-function relationship of IDRs.
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