Facultad de Ciencias, Departamento de Quimica Fisica, Universidad de Granada, 18071-Granada, Spain.
J Am Chem Soc. 2010 Feb 3;132(4):1218-9. doi: 10.1021/ja909298v.
Recent work has shown that proteins can tolerate hydrophobic-to-ionizable-residue mutations. Here, we provide experimental evidence that the essential properties (pK value, protonation state, local dynamics) of buried ionizable groups in proteins can be efficiently modulated through the rational design of the surface charge distribution, thus paving the way for the protein engineering exploitation of charge burial.
最近的研究表明，蛋白质可以耐受疏水性到离子化残基的突变。在这里，我们提供了实验证据，表明通过合理设计表面电荷分布，可以有效地调节蛋白质中埋置离子基团的基本性质（pK 值、质子化状态、局部动力学），从而为电荷埋藏的蛋白质工程利用铺平了道路。
