It is not known if both proteins are required for adequate heat shock protection. In order to test this, researchers will have to create mutant organisms having only one or the other protein to test which one is necessary, or whether, in fact, it is both. It is known that organisms can be somewhat adapted to withstand some heat shock. If a cell is subjected to slightly higher than optimal growing temperature, the thermosome is induced to turn on. Virtually all biological processes depend on enzymes, and enzymes are proteins.
All enzymes have a limited thermal range for which they function optimally.
Enzyme durability is often limited for other reasons besides temperature, such as gradual turnover, degradation, Enzyme stability is often limited outside the cell, which make their use on an industrial scale difficult. Because of their usefulness in catalysing chemical reactions, researchers are interested in learning more about increasing their stability. The mechanisms that make hypothermophiles thermostable are actually embedded as obvious structural features in the enzymes themselves. Protein structure is so complex and so intimately related to function that it is not possible to simply add features to a given protein to make it more thermostable. Researchers find it easier to go backwards, taking a complex protein and working backwards to understand its component features.