5,6-dimethoxy-2,3,4,4a,10,10a-hexahydro-1H-phenanthren-9-one | 111260-83-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 菲及其衍生物
• 英文名称: 5,6-dimethoxy-2,3,4,4a,10,10a-hexahydro-1H-phenanthren-9-one
• 英文别名: 5,6-dimethoxy-2,3,4,4a,10,10a-hexahydro-1H-phenanthren-9-one；5,6-Dimethoxy-2,3,4,4a,10,10a-hexahydro-1H-phenanthren-9-on
• CAS: 111260-83-4
• 化学式: C₁₆H₂₀O₃
• 分子量: 260.333
• InChiKey: YRMVNXVUUFWQLU-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：
  2.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  35.53
• 氢给体数：
  0.0
• 氢受体数：
  3.0

反应信息

• 作为产物：
  描述：

  溴乙酸乙酯 、 alkaline earth salt of/the/ methylsulfuric acid 在 甲苯 、 锌 作用下， 生成 5,6-dimethoxy-2,3,4,4a,10,10a-hexahydro-1H-phenanthren-9-one
  参考文献：
  名称：

  Analysis of the local conformation of proteins with two-dimensional fluorescence techniques

  摘要：

  Two 2D fluorescence techniques are described which allow the study of conformational changes in proteins in their native form in muM solutions using aromatic amino acids (tryptophan, tyrosine) as intrinsic fluorescence markers. Simultaneous time- and wavelength-resolved fluorescence spectra are measured using a 80 ps laser source in conjunction with streak detection in the exit plane of an astigmatism-corrected spectrometer. This approach allows identification of different photophysical processes by their associated lifetime and spectral intensity distribution; errors due to the more common integration over a wider spectral range are avoided. Time-resolved spectra are sensitive to changes in the collisional environment (dynamic quenching) and can thus be used to monitor local conformation changes close to the respective fluorophors. This is demonstrated for the Ras protein which undergoes a drastic conformation change while binding to different nucleotides.Excitation-emission spectra are two-dimensional fluorescence images with one axis corresponding to the excitation and the other to the emission wavelength. Thus, they contain all conventional excitation and fluorescence spectra of a given substance. The 2D structure facilitates the interpretation of these spectra and allows the direct identification of resonance effects, scattering and the isolation of the contribution of different fluorophors to the complete spectrum. This is demonstrated for mixtures of tyrosine and tryptophan, In this case, both wavelength-resolved spectra and temporal decays are affected by energy transfer processes between the two amino acids.In a last example, both static and time-resolved spectral methods are combined to determine the respective contribution of static and dynamic quenching in calsequestrin. Evaluation of the fluorescence data is in good agreement with a recent crystallographic analysis which shows that all tryptophans are located in a conserved domain of the protein. Addition of Ca2+ ions leads to a more compact form of calse-questrin and to polymers. This information would not be obtainable from either of the two techniques alone.

  DOI：

  10.1007/s003400000384

文献信息

• Analysis of the local conformation of proteins with two-dimensional fluorescence techniques
  作者：A. Brockhinke、R. Plessow、P. Dittrich、K. Kohse-Höinghaus

  DOI：10.1007/s003400000384

  日期：2000.11

  Two 2D fluorescence techniques are described which allow the study of conformational changes in proteins in their native form in muM solutions using aromatic amino acids (tryptophan, tyrosine) as intrinsic fluorescence markers. Simultaneous time- and wavelength-resolved fluorescence spectra are measured using a 80 ps laser source in conjunction with streak detection in the exit plane of an astigmatism-corrected spectrometer. This approach allows identification of different photophysical processes by their associated lifetime and spectral intensity distribution; errors due to the more common integration over a wider spectral range are avoided. Time-resolved spectra are sensitive to changes in the collisional environment (dynamic quenching) and can thus be used to monitor local conformation changes close to the respective fluorophors. This is demonstrated for the Ras protein which undergoes a drastic conformation change while binding to different nucleotides.Excitation-emission spectra are two-dimensional fluorescence images with one axis corresponding to the excitation and the other to the emission wavelength. Thus, they contain all conventional excitation and fluorescence spectra of a given substance. The 2D structure facilitates the interpretation of these spectra and allows the direct identification of resonance effects, scattering and the isolation of the contribution of different fluorophors to the complete spectrum. This is demonstrated for mixtures of tyrosine and tryptophan, In this case, both wavelength-resolved spectra and temporal decays are affected by energy transfer processes between the two amino acids.In a last example, both static and time-resolved spectral methods are combined to determine the respective contribution of static and dynamic quenching in calsequestrin. Evaluation of the fluorescence data is in good agreement with a recent crystallographic analysis which shows that all tryptophans are located in a conserved domain of the protein. Addition of Ca2+ ions leads to a more compact form of calse-questrin and to polymers. This information would not be obtainable from either of the two techniques alone.