The titled new complex was synthesized and determined by X-ray diffraction. The crystal belongs to monoclinic, P-I group, a=1.8997（4）nm, b-0.581 07（12）nm, c=2.4209（5）nm, β-90.65（3）°, V=2.672 2（9） nm^3,...The titled new complex was synthesized and determined by X-ray diffraction. The crystal belongs to monoclinic, P-I group, a=1.8997（4）nm, b-0.581 07（12）nm, c=2.4209（5）nm, β-90.65（3）°, V=2.672 2（9） nm^3, Z=4, Dc= 1.488 g/cm^3, It has C2 symmetry with the axis through the Zn atom, and the zinc atom is coordinated by two N atoms of the 1-（4-methoxyphenyl） 3-（ 1H-1, 2, 4-triazol-1-yl）-1-propanone ligands and two C1^- atoms, forming a slightly distorted tetrahedron. Intermolecular hydrogen bonds make the complex stable. IR and electronic spectra study of the target complex were also carried.展开更多
Experiments including C-13 spin-lattice relaxation, C-13 heteronuclear dipolar dephasing and H-1 spin diffusion are performed on poly (2,6-dimethyl-1,4-phenylene oxide) (PPO). The results show that the rotation of the...Experiments including C-13 spin-lattice relaxation, C-13 heteronuclear dipolar dephasing and H-1 spin diffusion are performed on poly (2,6-dimethyl-1,4-phenylene oxide) (PPO). The results show that the rotation of the methyl groups in solid PPO is partially restricted, which results in a surprisingly efficient spin diffusion between the aromatic proton and methyl proton characterized by a diffusion time of 150 mu s. The results also show that the aromatic ring in solid PPO is rigid and twisted, which causes all aromatic carbons to be chemically unequivalent.展开更多
The binding of nicotine to bovine serum albumin (BSA) was studied by UV absorption. fluorescence, and H-1 NMR methods. With the addition of nicotine, the absorption band of BSA at about 210 nm decreased gradually, mov...The binding of nicotine to bovine serum albumin (BSA) was studied by UV absorption. fluorescence, and H-1 NMR methods. With the addition of nicotine, the absorption band of BSA at about 210 nm decreased gradually, moved to longer wavelengths, and narrowed. BSA fluorescence of tryptophan residue was quenched by nicotine. The H-1 NMR peaks of nicotine moved to downfield by the addition of BSA. The experimental results showed that nicotine was capable of binding with BSA to form a 1:1 complex. BSA's high selectivity for nicotine binding suggests a unique role for this protein in the detoxification and/or transport of nicotine.展开更多
文摘The titled new complex was synthesized and determined by X-ray diffraction. The crystal belongs to monoclinic, P-I group, a=1.8997（4）nm, b-0.581 07（12）nm, c=2.4209（5）nm, β-90.65（3）°, V=2.672 2（9） nm^3, Z=4, Dc= 1.488 g/cm^3, It has C2 symmetry with the axis through the Zn atom, and the zinc atom is coordinated by two N atoms of the 1-（4-methoxyphenyl） 3-（ 1H-1, 2, 4-triazol-1-yl）-1-propanone ligands and two C1^- atoms, forming a slightly distorted tetrahedron. Intermolecular hydrogen bonds make the complex stable. IR and electronic spectra study of the target complex were also carried.
文摘Experiments including C-13 spin-lattice relaxation, C-13 heteronuclear dipolar dephasing and H-1 spin diffusion are performed on poly (2,6-dimethyl-1,4-phenylene oxide) (PPO). The results show that the rotation of the methyl groups in solid PPO is partially restricted, which results in a surprisingly efficient spin diffusion between the aromatic proton and methyl proton characterized by a diffusion time of 150 mu s. The results also show that the aromatic ring in solid PPO is rigid and twisted, which causes all aromatic carbons to be chemically unequivalent.
基金The National Natural Science Foundation of China Research Fund for Doctoral Program of Higher EducationProfessor Yuan Fa
文摘The binding of nicotine to bovine serum albumin (BSA) was studied by UV absorption. fluorescence, and H-1 NMR methods. With the addition of nicotine, the absorption band of BSA at about 210 nm decreased gradually, moved to longer wavelengths, and narrowed. BSA fluorescence of tryptophan residue was quenched by nicotine. The H-1 NMR peaks of nicotine moved to downfield by the addition of BSA. The experimental results showed that nicotine was capable of binding with BSA to form a 1:1 complex. BSA's high selectivity for nicotine binding suggests a unique role for this protein in the detoxification and/or transport of nicotine.
