1-(2-nitro-4,5-dimethoxyphenyl)ethane-1,2-diyl 1,2-dibromide | 113430-90-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 1-(2-nitro-4,5-dimethoxyphenyl)ethane-1,2-diyl 1,2-dibromide
• 英文别名: 1-(1,2-Dibromoethyl)-4,5-dimethoxy-2-nitrobenzene
• CAS: 113430-90-3
• 化学式: C₁₀H₁₁Br₂NO₄
• 分子量: 369.01
• InChiKey: NPIMWEWXFDNIGY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  17
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  64.3
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  1-(2-nitro-4,5-dimethoxyphenyl)ethane-1,2-diyl 1,2-dibromide 在 sodium hydroxide 作用下， 以 乙醇 为溶剂， 反应 504.0h， 生成
  参考文献：
  名称：

  A new class of photolabile chelators for the rapid release of divalent cations: generation of caged calcium and caged magnesium

  摘要：

  DOI：

  10.1021/jo00244a022
• 作为产物：
  描述：

  2-nitro-4,5-dimethoxystyrene 在 溴 作用下， 以 二氯甲烷 为溶剂， 以88%的产率得到1-(2-nitro-4,5-dimethoxyphenyl)ethane-1,2-diyl 1,2-dibromide
  参考文献：
  名称：

  Monitoring the Kinetics of Ion-Dependent Protein Folding by Time-Resolved NMR Spectroscopy at Atomic Resolution

  摘要：

  The kinetics of protein refolding have been monitored by time-resolved NMR spectroscopy. It is shown that refolding of metal binding proteins can be induced by photolysis of photo labile ion chelators, the subsequent release of Ca2+ ions can induce protein folding, and the changes in resonance positions can be monitored by time-resolved NMR spectroscopy. The feasibility of the approach is demonstrated by characterizing the refolding of alpha-lactalbumin, or protein containing a Ca2+ binding site, unfolded in 4 M urea at pH 7 in the absence of Ca2+. The refolding kinetics of the methyl groups of residues Leu15 and Val21 in the core of the protein have been determined to be mono-exponential with rates of 0.28 s(-1) and 0.23 s(-1), respectively at 300 K.

  DOI：

  10.1021/ja994212b

文献信息

• A new class of photolabile chelators for the rapid release of divalent cations: generation of caged calcium and caged magnesium
  作者：G. C. R. Ellis-Davies、J. H. Kaplan

  DOI：10.1021/jo00244a022

  日期：1988.4
• US4981985A
  申请人：——

  公开号：US4981985A

  公开（公告）日：1991-01-01
• Monitoring the Kinetics of Ion-Dependent Protein Folding by Time-Resolved NMR Spectroscopy at Atomic Resolution
  作者：Till Kühn、Harald Schwalbe

  DOI：10.1021/ja994212b

  日期：2000.7.1

  The kinetics of protein refolding have been monitored by time-resolved NMR spectroscopy. It is shown that refolding of metal binding proteins can be induced by photolysis of photo labile ion chelators, the subsequent release of Ca2+ ions can induce protein folding, and the changes in resonance positions can be monitored by time-resolved NMR spectroscopy. The feasibility of the approach is demonstrated by characterizing the refolding of alpha-lactalbumin, or protein containing a Ca2+ binding site, unfolded in 4 M urea at pH 7 in the absence of Ca2+. The refolding kinetics of the methyl groups of residues Leu15 and Val21 in the core of the protein have been determined to be mono-exponential with rates of 0.28 s(-1) and 0.23 s(-1), respectively at 300 K.