THE CORE LOOP INTERACTION THAT CONTROLS PROTEIN FOLDING

组装的多肽链折叠到 三维结构是许多学者深入研究的主题 实验室。我们采取了一种方法来破解这一后半段的 通过研究一种以前未知的非共价体的遗传密码 互动。我们前几年的研究表明，这种新的 交互以核心交互循环的形式存在于 折叠。如前几年所述，我们准备了类型1、2、4 来自马、金枪鱼、酵母iso-1或念珠菌的5个片段复合体 细胞色素c。不同的类型代表不同的部位。 多肽链的不连续。我们已经证明了亚铁血红素和 1、2、4或5型络合物的膜片完全可互换 在上述4个物种中的任何两个之间。此外，除了 两个H型杂化络合物，均为同源杂化1、2或5型 络合物表现出695 nm的吸收带。Y.P.Myer及其同事 已经表明，695 nm键，指示Met 80-S-血红素铁键， 监测Trp 59-血红素结构域的完整性。我们的结果表明， 695 nm波段还监测上述区域的结构完整性 在血红素的右边。识别该结构的单克隆4-128-6 以上酵母的血红素为异L-细胞色素c(见以前的报道)。 发现与AFL I和2类杂化络合物发生交叉反应，其中包含 酵母异-1-脱辅基蛋白或脱辅基蛋白。单抗474-6，识别 结构下面和左边的血红素(见以前的报告)是 还发现与类型1，但不与类型2的杂化络合物发生交叉反应 含有酵母iso-1凋亡素c.两种或两种以上的组合 突变发生在杂化复合体的右通道。右翼 R·E·迪克森和他的同事发现的通道是由近距离接触形成的 COOH-末端螺旋与NH2-末端螺旋和血红素的结合。因此， 结果表明，右声道的所有残留物很可能 可在两种真核细胞色素c的任意组合之间交换 物种。这反过来又表明， 右声道是保守的。因此，目前的研究指向 核心相互作用环在蛋白质折叠中的基本重要性。

The mechanism by which the assembled polypeptide chain folds to the three-dimensional structure is a subject of intensive studies in many laboratories. We have taken an approach to cracking this second half of the genetic code by investigating a previously unknown non-covalent interaction. Our studies in the previous years have suggested that such new interaction comes to existence in the form of core interaction loop after folding. As described in the previous years we have prepared Type 1, 2, 4 and 5 fragment complexes from horse, tuna, yeast iso-1 or Candida cytochrome c. The different types represent the different sites of the discontinuity of the polypeptide chain. We have shown that the heme and apofragments of Type 1, 2, 4 or 5 complexes are completely exchangeable between any two of the above 4 species. Furthermore, with the exception for two Type H hybrid complexes, all homologous and hybrid Type 1, 2 or 5 complexes exhibit the 695 nm absorbance band. Y. P. Myer and colleagues have shown that the 695 nm bond, indicative of the Met 80-S-heme Fe bond, monitors the integrity of the Trp 59-heme domain. Our results show that the 695 nm band also monitors the structural integrity of the regions above and to the right of heme. Monoclonal 4-128-6 which recognizes the structure above the heme of yeast iso-l -cytochrome c (see the previous reports) was found to cross react with afl Type I and 2 hybrid complexes containing yeast iso- 1 -apofragment or apoprotein. Monoclonal 474-6, recognizing the structure below and to the left of the heme (see the previous reports) was also found to cross react with aH Type 1, but not Type 2, hybrid complexes containing yeast iso- 1apocytochrome c. Combination of two or more mutations occurs in the right channel of the hybrid complexes. The right channel found by R. E. Dickerson and colleagues is formed by close contact of the COOH-terminal helix with the NH2- terminal helix and the heme. Thus, the results suggest that all residues of the right channel are likely exchangeable between any combination of two of eukaryotic cytochrome c species. This, in turn, suggests that the core interaction loop of the right channel is conserved. Thus, the present studies point to the fundamental importance of the core interaction loop in protein folding.