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首页> 外文期刊>Chemistry: A European journal >Dispersion Interactions Govern the Strong Thermal Stability of a Protein
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Dispersion Interactions Govern the Strong Thermal Stability of a Protein

机译：分散相互作用控制蛋白质的强热稳定性

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Rubredoxin from the hyper-thermophile Pyrococcus furiosus(Pf Rd)is an extremely thermostable protein,which makes it an attractive subject of protein folding and stability studies.A fundamental question arises as to what the reason for such extreme stability is and how it can be elucidated from a complex set of interatomic interactions.We addressed this issue first theoretically through a computational analysis of the hydrophobic core of the protein and its mutants,including the interactions taking place inside the core.Here we show that a single mutation of one of phenylalanine's residues inside the protein's hydrophobic core results in a dramatic decrease in its thermal stability.The calculated unfolding Gibbs energy as well as the sta- bilization energy differences between a few core residues follows the same trend as the melting temperature of protein variants determined experimentally by microcalorimetry measurements.NMR spectroscopy experiments have shown that the only part of the protein affected by mutation is the reasonably rearranged hydrophobic core.It is hence concluded that stabilization energies,which are dominated by London dispersion,represent the main source of stability of this protein.
机译：极热嗜热球菌Pr Rdocus（Pf Rd）的rubredoxin是一种极热稳定的蛋白质，这使其成为蛋白质折叠和稳定性研究的一个有吸引力的课题。我们从理论上首先通过对该蛋白及其突变体的疏水核的计算分析（包括在核内部发生的相互作用）从理论上解决了这一问题，在此我们证明了苯丙氨酸之一的单个突变蛋白质疏水核心内部的残基会导致其热稳定性急剧下降。计算出的展开吉布斯能以及少数核心残基之间的稳定能差异与通过微量热法实验确定的蛋白质变体的解链温度具有相同的趋势NMR光谱实验表明，受突变影响的蛋白质是合理重排的疏水核心。因此可以得出结论，以伦敦分散为主的稳定能是该蛋白质稳定的主要来源。

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