Disposition of polar and nonpolar residues on outer surfaces of transmembrane helical segments of proteins involved in proton translocation.
Disposition of polar and nonpolar residues on outer surfaces of transmembrane helical segments of proteins involved in proton translocation.
复制标题
参与质子易位的蛋白质跨膜螺旋片段外表面上极性和非极性残基的分布。
DOI：
10.1016/0003-9861(84)90334-5
复制
发表时间：
1984
影响因子：
3.9
通讯作者：
Senior,AE
中科院分区：
文献类型：
--
作者：
Senior,AE
“Helical wheel” projections of transmembrane helical segments of membrane proteins involved in proton translocation were constructed. The particular proteins studied were theuncFprotein subunit of theEscherichia coliproton-ATPase, theuncEprotein subunit of theE. coliproton-ATPase, and cytochrome oxidase subunit III. Clear demarcation of polar and nonpolar regions on surfaces of transmembrane helical segments was seen in theuncFprotein and inuncEprotein helical segment two, but not inuncEprotein helical segment one. The transmembrane segment of cytochrome oxidase subunit III which includes the dicyclohexylcarbodiimide (DCCD)-reactive residue was very similar toE. Coli uncEprotein helical segment two. The DCCD-reactive residue in both was clearly located on a nonpolar surface.
