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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Importance of main-chain hydrophobic free energy to the stability of thermophilic proteins
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Importance of main-chain hydrophobic free energy to the stability of thermophilic proteins

机译：主链疏水性自由能对嗜热蛋白稳定性的重要性

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摘要

Living organisms are found in the most unexpected places, including deep-sea vents at 100 degrees C and several hundred bars pressure, in hot springs. Needless to say, the proteins found in thermophilic species are much more stable than their mesophilic counterparts. There are no obvious reasons to say that one would be more stable than others. Even examination of the amino acids and comparison of structural features of thermophiles with mesophilies cannot bring satisfactory explanation for the thermal stability of such proteins. In order to bring out the hidden information behind the thermal stabilization of such proteins in terms of energy factors and their combinations, analysis were made on food resolution structures of thermophilic and their mesophilic homologous from 23 different families. From the structural coordinates, free energy contributions due to hydrophobic, electrostatic, hydrogen bonding, disulfide bonding and van der Waals interactions are computed. In this analysis. a vast majority of thermophilic proteins adopt slightly lower free energy contribution in each energy terms than its mesophilic counterparts. The major observation noted from this study is the lower hydrophobic free energy contribution due to carbon atoms and main-chain nitrogen atoms in all the thermophilic proteins. The possible combination of different free energy terms shows majority of the thermophilic proteins have lower free energy strategy than their mesophilic homologous. The derived results show that the hydrophobic free energy due to carbon and nitrogen atoms and Such combinations of free energy components play a vital role in the thermostablisation of such proteins. (c) 2005 Elsevier B.V. All rights reserved.
机译：在最出乎意料的地方发现了生物，包括温泉中100摄氏度和几百巴压力的深海喷口。不用说，嗜热菌种中的蛋白质比嗜温菌中的蛋白质稳定得多。没有明显的理由说一个人会比其他人更稳定。甚至对氨基酸的检测以及嗜热菌与嗜温菌的结构特征的比较也不能为此类蛋白质的热稳定性带来令人满意的解释。为了从能量因子及其组合的角度揭示此类蛋白热稳定背后的隐藏信息，对来自23个不同家族的嗜热菌及其嗜温同源物的食物分解结构进行了分析。从结构坐标计算出由于疏水，静电，氢键，二硫键和范德华相互作用而产生的自由能。在此分析。绝大多数嗜热蛋白在每种能量方面的自由能贡献都比其嗜温蛋白低。这项研究指出的主要观察结果是，由于所有嗜热蛋白中的碳原子和主链氮原子所致的疏水性自由能较低。不同自由能项的可能组合表明，大多数嗜热蛋白比其嗜温同源蛋白具有更低的自由能策略。得出的结果表明，由于碳和氮原子形成的疏水性自由能和自由能成分的这种组合在此类蛋白质的热稳定化中起着至关重要的作用。 （c）2005 Elsevier B.V.保留所有权利。

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