4-(6-甲氧基-5-甲基-[2]萘基)-丁酸 | 1029-76-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 中文名称: 4-(6-甲氧基-5-甲基-[2]萘基)-丁酸
• 英文名称: 4-(6-methoxy-5-methyl-[2]naphthyl)-butyric acid
• 英文别名: 4-<6-Methoxy-5-methyl-naphth-2-yl>-buttersaeure；4-(6-Methoxy-5-methyl-[2]naphthyl)-buttersaeure
• CAS: 1029-76-1
• 化学式: C₁₆H₁₈O₃
• 分子量: 258.317
• InChiKey: PXTDKHKNFUIVLP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.56
• 重原子数：
  19.0
• 可旋转键数：
  5.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  46.53
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  4-(6-甲氧基-5-甲基-[2]萘基)-丁酸 在 盐酸 、 selenium 、 amalgamated zinc 、 氢溴酸 、 四氯化锡 、 溶剂黄146 作用下， 生成 1-methylphenanthrol
  参考文献：
  名称：

  69.菲系列的合成。第一部分.2-甲氧基-1-甲基菲

  摘要：

  DOI：

  10.1039/jr9360000317
• 作为产物：
  描述：

  alkaline earth salt of/the/ methylsulfuric acid 在 盐酸 、 amalgamated zinc 作用下， 生成 4-(6-甲氧基-5-甲基-[2]萘基)-丁酸
  参考文献：
  名称：

  69.菲系列的合成。第一部分.2-甲氧基-1-甲基菲

  摘要：

  DOI：

  10.1039/jr9360000317

文献信息

• Mutations that alter the higher-order structure of its 5' untranslated region affect the stability of chloroplast rps7 mRNA
  作者：D. C. Fargo、E. Hu、J. E. Boynton、N. W. Gillham

  DOI：10.1007/s004380000321

  日期：2000.10

  In this paper, we examine the effects of mutations in the 5'UTR of the chloroplast rps7 transcript of Chlamydomonas reinhardtii that reduce the stability of the mRNA. Five point mutants in the rps7 5'UTR were selected on the basis of their failure to accumulate reporter mRNA in Escherichia coli. Each of these mutations produces alterations in the predicted higher-order structures of the rps7 5'UTR that destabilize the mRNA. Cis-acting suppressors of these mutations have been selected in E. coli and in the C. reinhardtii chloroplast that restore message stability and function. No differences in RNA melting and reannealing profiles have been observed between wild type, original mutant, and suppressor 5'UTRs transcribed in vitro. Proteins of 32 kDa and 47 kDa that bind to the wild-type rps7 5'UTR are not detected by UV cross-linking assays performed with any of the mutant rps7 5'UTRs. However, binding of the 32-kDa protein is restored in the six suppressor mutants examined. This suggests that the 32-kDa protein may be involved in protecting the rps7 5'UTR and the attached coding region from digestion by ribonucleases. Alternatively, the binding site for the 32-kDa protein may be independently lost in the rearranged tertiary structure of the mutant 5'UTR that exposes the RNA to degradation and is restored in the suppressor mutants.