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首页> 外文期刊>Journal of Molecular Biology >What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioninformatics analysis.
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What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioninformatics analysis.

机译：二硫键可以告诉我们有关蛋白质能量，功能和折叠的信息：模拟和生物信息学分析。

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摘要

We study the impact of disulfide bonds on protein stability and folding. Using lattice model simulations, we show that formation of a disulfide bond stabilizes a protein to an extent that depends on the distance along the chain between linked cysteine residues. However, the impact of disulfide bonds on folding kinetics varies broadly, from acceleration when disulfides are introduced in or close to the folding nucleus, to slowing when disulfides are introduced outside the nucleus. Having established the effect of disulfide bonds on stability, we study the correlation between the number of disulfide bonds and the composition of certain amino acid classes with the goal to use it as a statistical probe into factors that contribute to stability of proteins. We find that the number of disulfides is negatively correlated with aliphatic hydrophobic but not aromatic content. It is surprising that we observe a strong correlation of disulfide content with polar (Q,S,T,N) amino acid content and a strong negative correlation with charged (E,D,K,R) content. These findings provide insights into factors that determine protein stability and principles of protein design as well as possible relations of disulfide bonds and protein function. Copyright 2000 Academic Press.
机译：我们研究了二硫键对蛋白质稳定性和折叠的影响。使用晶格模型模拟，我们表明二硫键的形成将蛋白质稳定到一定程度，该程度取决于沿着连接的半胱氨酸残基之间的链的距离。但是，二硫化物键对折叠动力学的影响变化很大，从将二硫化物引入折叠核中或接近折叠核时的加速到将二硫化物引入核外时的减慢。建立了二硫键对稳定性的影响后，我们研究了二硫键的数量与某些氨基酸类别组成之间的相关性，目的是将其用作统计探查影响蛋白质稳定性的因素。我们发现二硫化物的数量与脂肪族疏水性呈负相关，但与芳香族含量无负相关。令人惊讶的是，我们观察到二硫键含量与极性（Q，S，T，N）氨基酸含量密切相关，而负电荷与带电（E，D，K，R）含量密切相关。这些发现为确定蛋白质稳定性和蛋白质设计原理以及二硫键与蛋白质功能之间可能关系的因素提供了见识。版权所有2000学术出版社。

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