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Protein stability and surface electrostatics: A charged relationship

机译：蛋白质稳定性和表面静电：带电关系

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摘要

Engineering proteins to withstand a broad range of conditions continues to be a coveted objective, holding the potential to advance biomedicine, industry, and our understanding of disease. One way of achieving this goal lies in elucidating the underlying interactions that define protein stability. It has been shown that the hydrophobic effect, hydrogen bonding, and packing interactions between residues in the protein interior are dominant factors that define protein stability. The role of surface residues in protein stability has received much less attention. It has been believed that surface residues are not important for protein stability particularly because their interactions with the solvent should be similar in the native and unfolded states. In the case of surface charged residues, it was sometimes argued that solvent exposure meant that the high dielectric of the solvent will further decrease the strength of the charge-charge interactions. In this paper, we challenge the notion that the surface charged residues are not important for protein stability. We computationally redesigned sequences of five different proteins to optimize the surface charge-charge interactions. All redesigned proteins exhibited a significant increase in stability relative to their parent proteins, as experimentally determined by circular dichroism spectroscopy and differential scanning calorimetry. These results suggest that surface charge-charge interactions are important for protein stability and that rational optimization of charge-charge interactions on the protein surface can be a viable strategy for enhancing protein stability.
机译：工程蛋白能够承受广泛的条件仍然是人们梦co以求的目标，具有促进生物医学，工业和我们对疾病理解的潜力。实现此目标的一种方法是阐明定义蛋白质稳定性的潜在相互作用。已经表明，蛋白质内部残基之间的疏水作用，氢键和堆积相互作用是决定蛋白质稳定性的主要因素。表面残基在蛋白质稳定性中的作用受到的关注很少。人们已经相信表面残基对于蛋白质的稳定性并不重要，特别是因为它们在天然和未折叠状态下与溶剂的相互作用应该相似。对于表面带电的残留物，有时会认为溶剂暴露意味着溶剂的高介电常数会进一步降低电荷-电荷相互作用的强度。在本文中，我们挑战了表面带电荷的残基对蛋白质稳定性不重要的观念。我们通过计算重新设计了五个不同蛋白质的序列，以优化表面​​电荷-电荷相互作用。通过圆二色光谱和差示扫描量热法实验确定，所有重新设计的蛋白质均相对于其亲本蛋白质表现出显着的稳定性。这些结果表明表面电荷-电荷相互作用对于蛋白质稳定性很重要，并且合理优化蛋白质表面上的电荷-电荷相互作用可以是增强蛋白质稳定性的可行策略。

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