Kohn W D, Kay C M, Hodges R S
Department of Biochemistry, University of Alberta, Edmonton, Canada.
J Mol Biol. 1997 Apr 11;267(4):1039-52. doi: 10.1006/jmbi.1997.0930.
An investigation into the role of surface-accessible ion pairs in protein stability was carried out by determining the effects of added salt (KCl, MgCl2 and LaCl3) at neutral and acidic pH on the stability of de novo designed two-stranded alpha-helical coiled-coils. The effects of salt on the stability of coiled-coils containing interhelical i to i' + 5 or intrahelical i to i + 4 and i to i + 3 Lys-Glu ion pairs were compared to the effects on the stability of a control coiled-coil, which contained no intra- or interhelical ion pair. These studies indicate that ionic interactions contribute to coiled-coil stability. The results show that added salt can have complex effects on protein stability, involving stabilizing and destabilizing contributions with the net effect depending on the nature of the charged residues and ionic interactions present in the protein.
通过测定在中性和酸性pH条件下添加盐(KCl、MgCl2和LaCl3)对从头设计的双链α-螺旋卷曲螺旋稳定性的影响,对表面可及离子对在蛋白质稳定性中的作用进行了研究。将盐对含有螺旋间i至i'+5或螺旋内i至i+4和i至i+3赖氨酸-谷氨酸离子对的卷曲螺旋稳定性的影响,与对不含螺旋内或螺旋间离子对的对照卷曲螺旋稳定性的影响进行了比较。这些研究表明离子相互作用有助于卷曲螺旋的稳定性。结果表明,添加的盐对蛋白质稳定性可能有复杂的影响,包括稳定和不稳定作用,其净效应取决于蛋白质中存在的带电残基的性质和离子相互作用。