ArticleBiophysical journal2006
Explanation of the stability of thermophilic proteins based on unique micromorphology.
Article in Biophysical journal, 2006. 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.
- Conformational Dynamics and Catalytic Backups in a Hyper-thermostable Engineered Archaeal Protein Tyrosine Phosphatase.JACS Au · 2026Article
- Thermostability engineering of industrial enzymes through structure modification.Applied microbiology and biotechnology · 2022Review
- Theoretical Development of DnaG Primase as a Novel Narrow-Spectrum Antibiotic Target.ACS omega · 2022Article
- Integrated Structural Studies for Elucidating Carotenoid-Protein Interactions.Advances in experimental medicine and biology · 2022Article
- X-ray radiolytic labeling reveals the molecular basis of orange carotenoid protein photoprotection and its interactions with fluorescence recovery protein.The Journal of biological chemistry · 2019Article
- Stabilizing HIV-1 envelope glycoprotein trimers to induce neutralizing antibodies.Retrovirology · 2018Review
- Stay Wet, Stay Stable? How Internal Water Helps the Stability of Thermophilic Proteins.The journal of physical chemistry. B · 2015Article
- Role of Internal Water on Protein Thermal Stability: The Case of Homologous G Domains.The journal of physical chemistry. B · 2015Article
- Stability curve prediction of homologous proteins using temperature-dependent statistical potentials.PLoS computational biology · 2014Article
- Thermophilic proteins: insight and perspective from in silico experiments.Chemical Society reviews · 2012Review
- Crowding induces differences in the diffusion of thermophilic and mesophilic proteins: a new look at neutron scattering results.Biophysical journal · 2011Article
- Thermo- and mesostabilizing protein interactions identified by temperature-dependent statistical potentials.Biophysical journal · 2010Article
- Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding.International journal of molecular sciences · 2009Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two mesophilic/thermophilic variants of the G-domain of the elongation factor Tu were studied via molecular dynamics simulations. By analyzing the simulation data via the Voronoi space tessellation, we have found that the two proteins have the same macromolecular packing, while the water-exposed surface area is larger for the thermophile. A larger coordination with water is probably due to a peculiar corrugation of the exposed surface of this species. From an enthalpic point of view, the thermophile shows a larger number of intramolecular hydrogen bonds, stronger electrostatic interactions, and a flatter free-energy landscape. Overall, the data suggest that the specific hydration state enhances macromolecular fluctuations but, at the same time, increases thermal stability.
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