ArticleProtein engineering, design & selection : PEDS2019
Information theoretic measures for quantifying sequence-ensemble relationships of intrinsically disordered proteins.
Article in Protein engineering, design & selection : PEDS, 2019. 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.
- Statistical Physics-Based Approaches to Model the Function and Complexation of Disordered Proteins.The journal of physical chemistry. B · 2025Article
- Physics-Based Machine Learning Trains Hamiltonians and Decodes the Sequence-Conformation Relation in the Disordered Proteome.Journal of chemical theory and computation · 2024Article
- Beyond monopole electrostatics in regulating conformations of intrinsically disordered proteins.PNAS nexus · 2024Article
- Design of intrinsically disordered protein variants with diverse structural properties.Science advances · 2024Article
- Machine-learning-based methods to generate conformational ensembles of disordered proteins.Biophysical journal · 2024Article
- Sequence-ensemble-function relationships for disordered proteins in live cells.bioRxiv : the preprint server for biology · 2023Article
- Design of intrinsically disordered protein variants with diverse structural properties.bioRxiv : the preprint server for biology · 2023Article
- Mechanosensitive ion channels MSL8, MSL9, and MSL10 have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics in vitro.Plant direct · 2023Article
- Phase Transitions of Associative Biomacromolecules.Chemical reviews · 2023Review
- Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Competing interactions give rise to two-state behavior and switch-like transitions in charge-rich intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Rules of Physical Mathematics Govern Intrinsically Disordered Proteins.Annual review of biophysics · 2022Review
- Uncovering Non-random Binary Patterns Within Sequences of Intrinsically Disordered Proteins.Journal of molecular biology · 2022Article
- Can sequence-specific and dynamics-based metrics allow us to decipher the function in IDP sequences?Biophysical journal · 2021Article
- Intrachain interaction topology can identify functionally similar intrinsically disordered proteins.Biophysical journal · 2021Article
- Engineering spatiotemporal organization and dynamics in synthetic cells.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021Review
- Dissecting the Functional Contributions of the Intrinsically Disordered C-terminal Tail of Bacillus subtilis FtsZ.Journal of molecular biology · 2020Article
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3 authors.
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Abstract
Intrinsically disordered proteins (IDPs) contribute to a multitude of functions. De novo design of IDPs should open the door to modulating functions and phenotypes controlled by these systems. Recent design efforts have focused on compositional biases and specific sequence patterns as the design features. Analysis of the impact of these designs on sequence-function relationships indicates that individual sequence/compositional parameters are insufficient for describing sequence-function relationships in IDPs. To remedy this problem, we have developed information theoretic measures for sequence-ensemble relationships (SERs) of IDPs. These measures rely on prior availability of statistically robust conformational ensembles derived from all atom simulations. We show that the measures we have developed are useful for comparing sequence-ensemble relationships even when sequence is poorly conserved. Based on our results, we propose that de novo designs of IDPs, guided by knowledge of their SERs, should provide improved insights into their sequence-ensemble-function relationships.
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