trustme.bro/r/…
✓ checked
trust me, bro:
here is the receipt.
the claim

Heat resistant proteins derive their stability from dense hydrophobic cores and salt bridges

the verdict
SUPPORTED
the evidence backs this
Recorded sources
4 sources for · 0 against

Counts group repeated records of the same source within each side. They do not measure evidence strength or source independence.

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.

The analysis

The retrieved literature consistently confirms that hydrophobic cores/clusters and salt bridges (ion pairs) are major structural determinants of thermal stability in thermophilic proteins. Papers [0], [2], [3], and [6] directly point to these two mechanisms as central to thermophilicity. There are no refuting papers, making the balance verdict SUPPORTED.

Evidence for · 4
Hydrophobic environment is a key factor for the stability of thermophilic proteins
Recorded source metadata

M. Michael Gromiha, Manish C. Pathak, Kadhirvel Saraboji, Eric A. Ortlund, Eric A. Gaucher. Hydrophobic environment is a key factor for the stability of thermophilic proteins. 2013. https://doi.org/10.1002/prot.24232

The study demonstrates that hydrophobic environments and ion pairs/salt bridges are major contributing factors to the thermal stability of thermophilic proteins.

See more details
More for · 3
Single Amino Acid Change Mutation in the Hydrophobic Core of the N-terminal Domain of P22 TSP affects the Proteins Stability
Recorded source metadata

Joseph A. Ayariga, Robert Villafane. Single Amino Acid Change Mutation in the Hydrophobic Core of the N-terminal Domain of P22 TSP affects the Proteins Stability. 2021. https://doi.org/10.1101/2021.12.16.472976

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.
Recorded source metadata

Dou Z, Wu X, Wan L, Gong B, Wang L. Structural Proteomics-Based Deciphering of Hydrophobic Packing Fingerprints Informing Protein Thermostability in TIM Barrels.. 2026. https://doi.org/10.1021/acs.jcim.6c01179

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.
Recorded source metadata

Alas-Guardado SJ, Anzures-Mendoza MS, Sol-Fragoso JY, López-Pérez E. Comparative Molecular Dynamics Study of the Thermal Stability of CheY Proteins from Hyperthermophilic and Mesophilic Organisms.. 2026. https://doi.org/10.1021/acs.jcim.5c02944

Molecular dynamics simulations show that enhanced thermal resistance in thermophilic proteins is mechanistically associated with an extensive network of stabilizing salt bridges.

The paper trail · every fact has a biography
first checked01 Aug 2026
judged → SUPPORTED · 8801 Aug 2026
Anyone with this link can read the claim and its public receipt, including any personal information in that text. Open permanent receipt.
Check your own claim
Challenge the receipt
Requests are recorded for review. This does not start an automatic check or guarantee a response time.
trust me, bro: win the argument, pass the class, survive peer review.

Citation formatting by citeproc-js (Frank Bennett) and the Citation Style Language project. Source and licenses.

This receipt is an automated verdict against our published method · not an opinion about any author or publication.
Terms · Privacy · How verdicts work · Dispute this receipt