Journal
JOURNAL OF PHYSICS-CONDENSED MATTER
Volume 22, Issue 32, Pages -Publisher
IOP PUBLISHING LTD
DOI: 10.1088/0953-8984/22/32/323101
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Funding
- European Union
- Region wallonne (Belgium)
- Fonds National de la Recherche Scientifique (Belgium)
- University of Liege
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Psychrophilic microorganisms thrive in permanently cold environments, even at subzero temperatures. To maintain metabolic rates compatible with sustained life, they have improved the dynamics of their protein structures, thereby enabling appropriate molecular motions required for biological activity at low temperatures. As a consequence of this structural flexibility, psychrophilic proteins are unstable and heat-labile. In the upper range of biological temperatures, thermophiles and hyperthermophiles grow at temperatures >100 degrees C and synthesize ultra-stable proteins. However, thermophilic enzymes are nearly inactive at room temperature as a result of their compactness and rigidity. At the molecular level, both types of extremophilic proteins have adapted the same structural factors, but in opposite directions, to address either activity at low temperatures or stability in hot environments. A model based on folding funnels is proposed accounting for the stability-activity relationships in extremophilic proteins.
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