ArticleFrontiers in molecular biosciences2022
The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes.
Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- Loop engineering of AtCas9 for effective and broad genome editing.Cell insight · 2025Article
- Structural mechanisms for cold-adapted activity of phosphoenolpyruvate carboxykinase.Protein science : a publication of the Protein Society · 2025Article
- Dynamically Interacting Protein Networks Provide a Mechanism to Overcome the Enormous Intrinsic Barrier to Orotidine 5'-Monophosphate Decarboxylation.ACS central science · 2025Article
- Phylogenetic history and temperature adaptation contribute to structural and functional stability of proteins in marine mollusks.Communications biology · 2025Article
- Identification of Scaffold Specific Energy Transfer Networks in the Enthalpic Activation of Orotidine 5'-Monophosphate Decarboxylase.bioRxiv : the preprint server for biology · 2025Article
- The Characterization of Ancient Methanococcales Malate Dehydrogenases Reveals That Strong Thermal Stability Prevents Unfolding Under Intense γ-Irradiation.Molecular biology and evolution · 2024Article
- Metal interactions of α-synuclein probed by NMR amide-proton exchange.Frontiers in chemistry · 2023Article
- Thermal tuning of protein hydration in a hyperthermophilic enzyme.Frontiers in molecular biosciences · 2022Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Proteins from hyperthermophilic organisms are evolutionary optimised to adopt functional structures and dynamics under conditions in which their mesophilic homologues are generally inactive or unfolded. Understanding the nature of such adaptation is of crucial interest to clarify the underlying mechanisms of biological activity in proteins. Here we measured NMR residual dipolar couplings of a hyperthermophilic acylphosphatase enzyme at 80°C and used these data to generate an accurate structural ensemble representative of its native state. The resulting energy landscape was compared to that obtained for a human homologue at 37°C, and additional NMR experiments were carried out to probe fast (
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