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Thermostability is the quality of a substance to resist irreversible change in its chemical or physical structure at a high relative temperature.
Thermostable materials may be used industrially as fire retardants. A thermostable plastic, an uncommon and unconventional term, is likely to refer to a thermosetting plastic that cannot be reshaped when heated, than to a thermoplastic that can be remelted and recast. Thermostability also commonly refers to a protein resistant to irreversible change in its protein structure due to applied heat.
Most life-forms on Earth live at temperatures of less than 50 °C, commonly from 15 to 50 °C. Above this, thermal energy may cause the unfolding of the protein structure to be irreversible, a condition understandably deleterious to continuing life-functions. The denaturing of proteins in albumen from a clear, nearly colourless liquid to an opaque white, insoluble gel is a common example of this.
Certain thermophilic life-forms exist which can withstand temperatures above this. Examining homologous proteins present in these thermophiles and other organisms reveal only slight differences in the protein structure. One notable difference is the presence of extra hydrogen bonds in the thermophile's proteins—meaning that the protein structure is more resistant to unfolding. The presence of certain types of salt has been observed to decrease thermostability in the proteins of mesophiles but not of hyperthermophiles which may indicate that salt bridges have more impact on thermostability at high temperature than is currently widely acknowledged. Another factors of protein thermostability are compactness of protein structure, oligomerization, and strength interaction between subunits.
Certain poisonous fungi contain thermostable toxins, such as amatoxin found in the death cap and autumn skullcap mushrooms. Therefore, applying heat to these deadly mushrooms will not remove its toxicity.
|Thermoregulation in animals|
|Ectotherm • Endotherm • Poikilotherm • Homeothermy • Heterothermy • Stenotherm • Eurytherm • Thermolabile • Thermostability • Gigantothermy • Kleptothermy • Bradymetabolism • Tachymetabolism|
- A Comparison of the Thermostability of Glyceraldehyde 3-phosphate Dehydrogenase From Thermophiles and Mesophiles in Different Ionic Salt Solutions
- Preferred amino acids and thermostability
- Thermostability of Proteins
- Salt Bridges
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