Ohmura T, Ueda T, Ootsuka K, Saito M, Imoto T
Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan.
Protein Sci. 2001 Feb;10(2):313-20. doi: 10.1110/ps.37401.
Stabilization of a protein using cavity-filling strategy has hardly been successful because of unfavorable van der Waals contacts. We succeeded in stabilizing lysozymes by cavity-filling mutations. The mutations were checked by a simple energy minimization in advance. It was shown clearly that the sum of free energy change caused by the hydrophobicity and the cavity size was correlated very well with protein stability. We also considered the aromatic-aromatic interaction. It is reconfirmed that the cavity-filling mutation in a hydrophobic core is a very useful method to stabilize a protein when the mutation candidate is selected carefully.
由于不利的范德华接触，使用空穴填充策略来稳定蛋白质几乎没有成功过。我们通过空穴填充突变成功地稳定了溶菌酶。这些突变预先通过简单的能量最小化进行了检查。结果清楚地表明，由疏水性和空穴大小引起的自由能变化之和与蛋白质稳定性非常相关。我们还考虑了芳香-芳香相互作用。再次证实，当仔细选择突变候选物时，在疏水核心进行空穴填充突变是稳定蛋白质的一种非常有用的方法。
