ArticleStructure (London, England : 1993)2008
Predicting the energetics of conformational fluctuations in proteins from sequence: a strategy for profiling the proteome.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Ensemble molecular mimicry correlates with antibody cross-reactivity in proteome-wide studies.Frontiers in immunology · 2026Article
- A Thermodynamic Atlas of Proteomes Reveals Energetic Innovation across the Tree of Life.Molecular biology and evolution · 2022Article
- Conserved allosteric ensembles in disordered proteins using TROSY/anti-TROSY RBiophysical journal · 2021Article
- Convergent Evolution and Structural Adaptation to the Deep Ocean in the Protein-Folding Chaperonin CCTα.Genome biology and evolution · 2020Article
- Hidden dynamic signatures drive substrate selectivity in the disordered phosphoproteome.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Sequence-Based Analysis of Thermal Adaptation and Protein Energy Landscapes in an Invasive Blue Mussel (Mytilus galloprovincialis).Genome biology and evolution · 2017Article
- A horizontal alignment tool for numerical trend discovery in sequence data: application to protein hydropathy.PLoS computational biology · 2013Article
- PROTS: a fragment based protein thermo-stability potential.Proteins · 2012Article
- Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors.The Journal of biological chemistry · 2011Review
- The role of protein conformational fluctuations in allostery, function, and evolution.Biophysical chemistry · 2011Review
- Sequence-based analysis of protein energy landscapes reveals nonuniform thermal adaptation within the proteome.Molecular biology and evolution · 2009Article
- Energetic profiling of protein folds.Methods in enzymology · 2009Article
- Article
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Authors and funding
2 authors.
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Abstract
The abundance of dynamic and disordered regions in proteins suggests that structural determinants alone may not be sufficient to describe function. Instead, descriptors that account for the dynamic features of the energy landscape populated by the protein ensemble may be required. Here, we show that the thermodynamics of the dynamical complexity that imparts biological function can be largely reconstructed using sequence information alone, allowing thermodynamic characterization of entire proteomes without the need for structural analysis. We show that this tool can be used to analyze conserved energetic signatures within classes of proteins, as well as to compare the thermodynamic character of different proteomes.
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Registered trials
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