Heat resistant proteins derive their stability from dense hydrophobic cores and salt bridges
the verdict
SUPPORTED
the evidence backs this
confidence 88/100
Heat resistant (thermophilic) proteins derive their enhanced structural stability primarily from densely packed hydrophobic cores and extensive networks of salt bridges, as supported by multiple structural analyses and molecular dynamics studies.
Evidence for · 4
Hydrophobic environment is a key factor for the stability of thermophilic proteins
2013 · cited by 126
The study demonstrates that hydrophobic environments and ion pairs/salt bridges are major contributing factors to the thermal stability of thermophilic proteins.
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More for · 3
Single Amino Acid Change Mutation in the Hydrophobic Core of the N-terminal Domain of P22 TSP affects the Proteins Stability
2021 · cited by 4
Mutagenesis of the hydrophobic core of the N-terminal domain significantly affects protein stability, proving its essential role.
Structural Proteomics-Based Deciphering of Hydrophobic Packing Fingerprints Informing Protein Thermostability in TIM Barrels.
2026 · cited by 0
Analysis of TIM barrels reveals that thermophilic proteins exhibit larger and more densely packed hydrophobic clusters compared to nonthermophilic counterparts.
Comparative Molecular Dynamics Study of the Thermal Stability of CheY Proteins from Hyperthermophilic and Mesophilic Organisms.
2026 · cited by 0
Molecular dynamics simulations show that enhanced thermal resistance in thermophilic proteins is mechanistically associated with an extensive network of stabilizing salt bridges.