Jaenicke R, Závodszky P
Institute of Biophysics and Physical Biochemistry, University of Regensburg, FRG.
FEBS Lett. 1990 Aug 1;268(2):344-9. doi: 10.1016/0014-5793(90)81283-t.
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.
地球上的生命在温度从-5到110摄氏度、静水压力从0.1到120兆帕、水分活度从1.0到0.6以及pH值从1到12的范围内无处不在。一般来说，蛋白质对不断变化的环境条件的适应性变化倾向于在整体拓扑结构、柔韧性和水合作用方面维持“相应状态”。由于负责增强稳定性的稳定自由能的微小变化，自然界提供了各种各样不同的适应性策略。就嗜热蛋白质而言，提高堆积密度至关重要。对于嗜盐蛋白质，降低疏水性和聚集表面电荷有助于增加在高盐浓度下溶解所需的水和盐结合。就嗜压微生物而言，高压适应性预计不如适应控制深海的低温那么重要。关于嗜冷和嗜酸/嗜碱适应性的潜在机制尚不清楚。
