Chin C N, von Heijne G
Department of Biochemistry, Stockholm University, Stockholm, S-106 91, Sweden.
J Mol Biol. 2000 Oct 13;303(1):1-5. doi: 10.1006/jmbi.2000.4122.
We have examined the effects of Lys-Asp charge pair interactions on the position of a model poly-Leu transmembrane helix in the ER membrane using the so-called "glycosylation mapping" technique. Based on an analysis of a set of constructs containing pairs of positively charged Lys and negatively charged Asp residues in various positions in the model helix, we show that the helix is located deeper in the membrane when Lys and Asp are placed one helical turn apart than for other spacings of the two residues. These results suggest that salt-bridge formation between residues located on the same face of a transmembrane helix may reduce the free energy of membrane partitioning.
我们使用所谓的“糖基化定位”技术，研究了赖氨酸-天冬氨酸电荷对相互作用对内质网（ER）膜中模型多聚亮氨酸跨膜螺旋位置的影响。基于对一组构建体的分析，这些构建体在模型螺旋的不同位置包含带正电荷的赖氨酸和带负电荷的天冬氨酸残基对，我们发现，当赖氨酸和天冬氨酸相隔一个螺旋圈放置时，螺旋在膜中的位置比这两个残基的其他间距更深。这些结果表明，位于跨膜螺旋同一面上的残基之间形成盐桥可能会降低膜分配的自由能。
