Little M, Ludueña R F
Biochim Biophys Acta. 1987 Mar 18;912(1):28-33. doi: 10.1016/0167-4838(87)90243-3.
Two cysteines of the major neuronal beta-tubulin subunit (beta 1) can be specifically cross-linked with the bifunctional sulfhydryl reagent N',N'-ethylenebis(iodoacetamide) after removal of GTP. A cysteine in position 12 cross-links with one of the cysteines in position 201 or 211. Although the two cross-linked cysteines are separated by at least 189 residues in the primary structure of tubulin, they are maximally 9 A apart in the tertiary structure.
去除鸟苷三磷酸(GTP)后,主要神经元β-微管蛋白亚基(β1)的两个半胱氨酸可与双功能巯基试剂N',N'-亚乙基双(碘乙酰胺)特异性交联。第12位的一个半胱氨酸与第201位或211位的一个半胱氨酸交联。尽管在微管蛋白一级结构中,这两个交联的半胱氨酸被至少189个残基隔开,但在三级结构中它们相距最大为9埃。