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Detection and Comparison of Structure and Function of Wild-type Pneumolysin and Its Novel Mutant PIyM2

Chemical Research in Chinese Universities 2015年第4期31卷 553-557页

作者： SUN Tianxu HOU Hongjia LU Jingcai XU Man GU Tiejun WANG Dandan DONG Yunliang JIANG Chunlai KONG Wei WUYongge National Engineering Laboratory for Aids Vaccine School of Life Science Jilin University Changchun 130012 P. R. China

Here is reported a novel pneumolysin（Ply） mutant（PlyM2） that addresses a long-standing problem for vaccine development in this field： detoxification of Ply in the premise of retaining antigenic integrity. Structure and function of wild-type Ply（PIyWT） and PIyM2 mutants were detected and compared. Their structures were not signi- ficantly different according to the analysis by thermal-dependent fluorescence spectroscopy and circular dichroism spectroscopy. PlyM2 was confirmed to have lost hemolytic activity and yet could induce neutralizing antibodies to prevent in vitro hemolysis by PIyWT and Streptococcus pneumoniae（S, pneumoniae）. These results give support to PIyM2 to be a new protein antigen for inclusion in the development of an effective pneumocoecal multiprotein vaccine.

关键词： Pneumolysin circular dichroism spectroscopy Thermal-dependent fluorescence spectroscopy Strepto-coccus pneumoniae Detoxification Mutation

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Effect of a Single Repeat Sequence of the Human Telomere d（TTAGGG）on Structure of Single-Stranded Telomeric DNA d[AGGG（TTAGGG）6]

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Chinese Journal of Chemical Physics 2018年第5期31卷 635-640,735页

作者： Tian-lei Guang Ya-ting Gao Xiao-dong Ye Hefei National Laboratory for Physical Sciences at the Microscale Department of Chemical PhysicsUniversity of Science and Technology of ChinaHefei 230026China CAS Key Laboratory of Soft Matter Chemistry University of Science and Technology of ChinaHefei 230026China

The structures of human telomeric DNA have received much attention due to its significant biological *** studies have focused on G-quadruplex structure formed by short telomeric DNA sequence,but little is known about the structures of long singlestranded telomeric ***,we investigated the structure of DNA with a long sequence of d[AGGG(TTAGGG)6](G6-DNA)and the effect of a single repeat sequence d(TTAGGG)(G01-DNA)on the structure of G6-DNA using sedimentation velocity technique,polyacrylamide gel electrophoresis,circular dichroism spectroscopy,and UV melting *** results suggest that the G6-DNA can form dimers in aqueous solutions and G01-DNA can form additional G-quadruplex structures by binding to ***,G01-DNA has no effect on the structure of DNA with a sequence of d[AGGG(TTAGGG)3](G3-DNA).Our study provides new insights into the structure polymorphism of long human single-stranded telomeric DNA.

关键词： circular dichroism spectroscopy G-guadruplex Sedimentation velocity experiments

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Different Thermostability of Skeletal Muscle Glyceraldehyde-3-phosphate Dehydrogenase from Hibernating and Euthermic Jerboa (Jaculus orientalis)

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Acta Biochimica et Biophysica Sinica 2003年第10期35卷 891-896页

作者： IDDAR Abdelghani,CAMPOS Luis A.,SANCHO Javier,SERRANO Aurelio,SOUKRI Abdelaziz Laboratoire de Biochimie Departamento de Bioquímica y Biología Molecular y Celular Departamento de Bioquímica y Biología Molecular y Celular Instituto de Bioquímica Vegetal y Fotosíntesis Laboratoire de Biochimie Unitè de Gènie Enzymatique et Biologie Molèculaire Facultè des Sciences-Ain Chock Casablanca Morocco Universidad de Zaragoza Zaragoza Spain Universidad de Zaragoza Zaragoza Spain CSIC-Universidad de Sevilla Sevilla Spain Unitè de Gènie Enzymatique et Biologie Molèculaire Facultè des Sciences-Ain Chock Casablanca Morocco

In previous study, we demonstrated that the specific activity of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.***.1.12) in skeletal muscle of induced hibernating jerboa (hibernating GAPDH) was 3-4 folds lower than that of the one in the skeletal muscle of the euthermic jerboa (euthermic GAPDH). A significant decrease in both GAPDH protein and GapC mRNA levels occurs when hibernating, but the purified hibernating GAPDH is less active than the euthermic GAPDH. To investigate the physico-chemical basis of this lower activity, the behaviour during thermal inactivation of skeletal muscle GAPDH from hibernating and euthermic tissues was examined by a variety of spectroscopic techniques, including fluorescence emission, circular dichroism and ultraviolet absorption. A clear resistance to thermal denaturation was observed in the hibernating GAPDH compared with the euthermic GAPDH. The different temperature of denaturation found in these proteins by both fluorimetry and circular dichroism indicates that there might exist conformational changes of GAPDH upon hibernation that could affect the stability of this enzyme.

关键词： glyceraldehyde-3-phosphate dehydrogenase hibernation thermal denaturation circular dichroism spectroscopy protein stability

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