ArticleThe journal of physical chemistry. B2023
Structural Preferences Shape the Entropic Force of Disordered Protein Ensembles.
Article in The journal of physical chemistry. B, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Experimental Data Driven AI Framework for Flexible Protein Conformational Reconstruction.bioRxiv : the preprint server for biology · 2026Article
- Predicting Pose Distribution of Protein Domains Connected by Flexible Linkers Is an Unsolved Problem.Proteins · 2026Article
- The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking.Nature structural & molecular biology · 2025Article
- AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.Protein science : a publication of the Protein Society · 2025Article
- Systematic analysis of structural disorder in the minimal proteome ofMicrobiology spectrum · 2025Article
- Glycosylation Weakens Skp1 Homodimerization inBiochemistry · 2025Article
- Advances in uncovering the mechanisms of macromolecular conformational entropy.Nature chemical biology · 2025Review
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- Controlled by disorder: Phosphorylation modulates SRSF1 domain availability for spliceosome assembly.Protein science : a publication of the Protein Society · 2025Article
- Amino Acid Residue-Specific Ramachandran Distributions Derived from a Simple Mean Field Potential.ACS physical chemistry Au · 2024Article
- A coarse-grained model for disordered and multi-domain proteins.Protein science : a publication of the Protein Society · 2024Article
- Intrinsically disordered region amplifies membrane remodeling to augment selective ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Correlating Disordered Activation Domain Ensembles with Gene Expression Levels.bioRxiv : the preprint server for biology · 2024Article
- Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Intrinsically disordered regions are poised to act as sensors of cellular chemistry.Trends in biochemical sciences · 2023Review
- IndiSPENsable for X Chromosome Inactivation and Gene Silencing.Epigenomes · 2023Review
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Abstract
Intrinsically disordered protein regions (IDRs) make up over 30% of the human proteome and exist in a dynamic conformational ensemble instead of a native, well-folded structure. Tethering IDRs to a surface (for example, the surface of a well-folded region of the same protein) can reduce the number of accessible conformations in these ensembles. This reduces the ensemble's conformational entropy, generating an effective entropic force that pulls away from the point of tethering. Recent experimental work has shown that this entropic force causes measurable, physiologically relevant changes to protein function. But how the magnitude of this force depends on IDR sequence remains unexplored. Here, we use all-atom simulations to analyze how structural preferences in IDR ensembles contribute to the entropic force they exert upon tethering. We show that sequence-encoded structural preferences play an important role in determining the magnitude of this force: compact, spherical ensembles generate an entropic force that can be several times higher than more extended ensembles. We further show that changes in the surrounding solution's chemistry can modulate the IDR entropic force strength. We propose that the entropic force is a sequence-dependent, environmentally tunable property of terminal IDR sequences.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.