Detailed circular dichroism(CD) and Fourier transform infrared(FTIR) studies have been carried out to monitor thermal unfolding of horseradish peroxidase isoenzyme C(HRP) inhibited by CN -(HRP CN). The results suggest...Detailed circular dichroism(CD) and Fourier transform infrared(FTIR) studies have been carried out to monitor thermal unfolding of horseradish peroxidase isoenzyme C(HRP) inhibited by CN -(HRP CN). The results suggest that HRP CN is quite different from native HRP with different spin states of Fe of heme and different coordinated states. Cyanide becomes the sixth ligand of Fe(Ⅲ) of heme and the hydrogen binding network is destroyed partly at the same time, which cause the drastic decrease of thermal stability of HRP. The FTIR and Soret CD spectra analysis demonstrate that during the heating process there is an intermediate state(I) which has both partly destroyed secondary and tertiary structures of native HRP, then it is the appearance of protein aggregation state(A) after fully unfolding. The unfolding pathway thus can be shown as follows: IIUA.展开更多
A new chiral conjugated polymer was synthesized by the Wittig-Horner polymerization of optically active binaphthyl monomer at the 3,3-positions. The circular dichroism spectrum of the polymer shows that the degree o...A new chiral conjugated polymer was synthesized by the Wittig-Horner polymerization of optically active binaphthyl monomer at the 3,3-positions. The circular dichroism spectrum of the polymer shows that the degree of circular polarization in absorption, g_ abs, is 1.9×10 -3 in chloroform at room temperature. The circularly polarized photoluminescence spectrum of the polymer shows that the degree of circular polarization in emission, g_ lum, is -1.6×10 -3 in chloroform at room temperature. As the polymer is readily soluble in chloroform, the results indicate that the circular polarization in absorption and emission is originated from molecularly dissolved chains and is due to exciton coupling between chain segments of the same polymer molecule. The results also show that the polymer could emit partially circularly polarized light when irradiated in chloroform at room temperature.展开更多
文摘Detailed circular dichroism(CD) and Fourier transform infrared(FTIR) studies have been carried out to monitor thermal unfolding of horseradish peroxidase isoenzyme C(HRP) inhibited by CN -(HRP CN). The results suggest that HRP CN is quite different from native HRP with different spin states of Fe of heme and different coordinated states. Cyanide becomes the sixth ligand of Fe(Ⅲ) of heme and the hydrogen binding network is destroyed partly at the same time, which cause the drastic decrease of thermal stability of HRP. The FTIR and Soret CD spectra analysis demonstrate that during the heating process there is an intermediate state(I) which has both partly destroyed secondary and tertiary structures of native HRP, then it is the appearance of protein aggregation state(A) after fully unfolding. The unfolding pathway thus can be shown as follows: IIUA.
文摘A new chiral conjugated polymer was synthesized by the Wittig-Horner polymerization of optically active binaphthyl monomer at the 3,3-positions. The circular dichroism spectrum of the polymer shows that the degree of circular polarization in absorption, g_ abs, is 1.9×10 -3 in chloroform at room temperature. The circularly polarized photoluminescence spectrum of the polymer shows that the degree of circular polarization in emission, g_ lum, is -1.6×10 -3 in chloroform at room temperature. As the polymer is readily soluble in chloroform, the results indicate that the circular polarization in absorption and emission is originated from molecularly dissolved chains and is due to exciton coupling between chain segments of the same polymer molecule. The results also show that the polymer could emit partially circularly polarized light when irradiated in chloroform at room temperature.
