Proteins under extreme physical conditions.
Life on earth is ubiquitous within the limits from -5 to 110 degrees C for temperature, 0.1 to 120 MPa for hydrostatic pressure, 1.0 to 0.6 for water activity and pH 1 to 12. In general, mutative adaptation of proteins to changing environmental conditions tends to maintain 'corresponding states' regarding overall topology, flexibility and hydration. Due to the minute changes in the free energy of stabilization responsible for enhanced stability, nature provides a wide variety of different adaptative strategies. In the case of thermophilic proteins, improved packing densities are crucial. In halophilic proteins, decreased hydrophobicity and clustered surface charges serve to increase water and salt binding required for solubilization at high salt concentration. In the case of barophiles, high-pressure adaptation is expected to be less important than adaptation to low temperatures governing the deep sea. Nothing is known with respect to the mechanisms underlying psychrophilic and acidophilic/alkalophilic adaptation.
Institute of Biophysics and Physical Biochemistry, University of Regensburg, FRG.
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Jaenicke
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Závodszky
D000222:Adaptation, Physiological; D001426:Bacterial Proteins; D003080:Cold Temperature; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006874:Hydrostatic Pressure; D009154:Mutation; D009994:Osmolar Concentration; D011487:Protein Conformation; D011506:Proteins; D013816:Thermodynamics
D001426:Bacterial Proteins; D011506:Proteins