In this paper,on the basis of making full use of the characteristics of unconstrained generalized geometric programming（GGP）,we establish a nonmonotonic trust region algorithm via the conjugate path for solving unco...In this paper,on the basis of making full use of the characteristics of unconstrained generalized geometric programming（GGP）,we establish a nonmonotonic trust region algorithm via the conjugate path for solving unconstrained GGP problem.A new type of condensation problem is presented,then a particular conjugate path is constructed for the problem,along which we get the approximate solution of the problem by nonmonotonic trust region algorithm,and further prove that the algorithm has global convergence and quadratic convergence properties.展开更多
Ancylostoma anticoagulant peptide 5 （AcAP5） is a strong inhibitor of human coagulation factor Xa （FXa）. The N-terminal residues （N40） of AcAP5 contains a domain that could combine with FXa. In order to determine...Ancylostoma anticoagulant peptide 5 （AcAP5） is a strong inhibitor of human coagulation factor Xa （FXa）. The N-terminal residues （N40） of AcAP5 contains a domain that could combine with FXa. In order to determine whether N40 protein has FXa inhibitory effect, we cloned, expressed and purified the protein for activity evaluation. The DNA fragment coding N40 was amplified by PCR, cloned into pET-30a to construct recombinant plasmid pET30a-N40, and subsequently transformed into E. coli, BL21 （DE3）. Expression of N40 was induced by isopropyl ~3-D-l-thiogalactopyranoside （IPTG）, and the interest protein was identified by SDS-PAGE and purified using one-step nickel （Ni） affinity chromatography. Under the optimal expres- sion condition （0.05 mM IPTG for 6 h at 37 ℃）, the purity of N40 reached 90%. We also evaluated the inhibition activity of N40 protein on FXa, finding the ICso was 4.58× 10 5 mol/L, This study suggests the N40 of AcAP5 could combine with FXa to inhibit FXa activity.展开更多
Kynurenine aminotransferases （KATs） catalyze the transamination of kynurenine （KYN） pathway and endogenous KYNs have been suggested to highly correlate to abnormal brain diseases. HKAT3 is a key member of KAT fami...Kynurenine aminotransferases （KATs） catalyze the transamination of kynurenine （KYN） pathway and endogenous KYNs have been suggested to highly correlate to abnormal brain diseases. HKAT3 is a key member of KAT family, while the binding mechanism of KYN and cofactor with HKAT3 has not been determined yet. In this study, we focus on the structure-function relationship among KYN, cofactor and HKAT3. The binding models of KYN complex and KYN＆cofactor complex were ob- tained and were studied by molecular dynamics （MD） simulations. We identified several critical residues and influence of conformational changes in human kynurenine aminotransferase 3 （HKAT3） complexes. The cofactor may contribute largely not only to the catalysis, but also to the binding. In addition, a hypothesis is proposed that a strong hydrophobic interaction between Tyr159 and Lys280 may influence the binding mode and the binding region of the substrate and the cofactor. Our re- suits will be a good starting point for further determination of the biological role.展开更多
Hydrophobic fluorescence:Tan and his colleagues recently introduced a brand new chemotype of environment-sensitive fluorescent turn-on probes to detect the hydrophobic ligand-binding domain by using SBD fluorophore.Th...Hydrophobic fluorescence:Tan and his colleagues recently introduced a brand new chemotype of environment-sensitive fluorescent turn-on probes to detect the hydrophobic ligand-binding domain by using SBD fluorophore.The design strategy described in this report generalized the environment sensitivity turn-on mechanism to recognize a specific protein,which provides a robust breakthrough for interchanging fluorescence in conventional small-molecule fluorescent imaging.展开更多
基金Supported by the National Science Foundation of China（10671126） Supported by the Shanghai Municipal Government Project（S30501）+3 种基金 Supported by the Innovation Fund Project for Graduate Student of Shanghai（JWCXSL1001） Supported by the Youth Foundation of Henan Polytechnic University（Q20093） Supported by the Applied Mathematics Provinciallevel Key Discipline of Henan Province Supported by Operational Research and Control Theory Key Discipline of Henan Polytechnic University
文摘In this paper,on the basis of making full use of the characteristics of unconstrained generalized geometric programming（GGP）,we establish a nonmonotonic trust region algorithm via the conjugate path for solving unconstrained GGP problem.A new type of condensation problem is presented,then a particular conjugate path is constructed for the problem,along which we get the approximate solution of the problem by nonmonotonic trust region algorithm,and further prove that the algorithm has global convergence and quadratic convergence properties.
基金National Technology Graveness Special Purpose Fund (Grant No. 2009zx09301-010)
文摘Ancylostoma anticoagulant peptide 5 （AcAP5） is a strong inhibitor of human coagulation factor Xa （FXa）. The N-terminal residues （N40） of AcAP5 contains a domain that could combine with FXa. In order to determine whether N40 protein has FXa inhibitory effect, we cloned, expressed and purified the protein for activity evaluation. The DNA fragment coding N40 was amplified by PCR, cloned into pET-30a to construct recombinant plasmid pET30a-N40, and subsequently transformed into E. coli, BL21 （DE3）. Expression of N40 was induced by isopropyl ~3-D-l-thiogalactopyranoside （IPTG）, and the interest protein was identified by SDS-PAGE and purified using one-step nickel （Ni） affinity chromatography. Under the optimal expres- sion condition （0.05 mM IPTG for 6 h at 37 ℃）, the purity of N40 reached 90%. We also evaluated the inhibition activity of N40 protein on FXa, finding the ICso was 4.58× 10 5 mol/L, This study suggests the N40 of AcAP5 could combine with FXa to inhibit FXa activity.
基金supported by the National Natural Science Foundation of ChinaSpecialized Research Fund for the Doctoral Program of Higher EducationSpecialized Fund for the Basic Research of Jilin University (20903045, 20573042, 20070183046,200810018)
文摘Kynurenine aminotransferases （KATs） catalyze the transamination of kynurenine （KYN） pathway and endogenous KYNs have been suggested to highly correlate to abnormal brain diseases. HKAT3 is a key member of KAT family, while the binding mechanism of KYN and cofactor with HKAT3 has not been determined yet. In this study, we focus on the structure-function relationship among KYN, cofactor and HKAT3. The binding models of KYN complex and KYN＆cofactor complex were ob- tained and were studied by molecular dynamics （MD） simulations. We identified several critical residues and influence of conformational changes in human kynurenine aminotransferase 3 （HKAT3） complexes. The cofactor may contribute largely not only to the catalysis, but also to the binding. In addition, a hypothesis is proposed that a strong hydrophobic interaction between Tyr159 and Lys280 may influence the binding mode and the binding region of the substrate and the cofactor. Our re- suits will be a good starting point for further determination of the biological role.
基金supported by the National Natural Science Foundation of China (81370085)the Program of New Century Excellent Talents in University (NCET-11-0306)+2 种基金the Fok Ying Tong Education Foundation (122036)the Shandong Natural Science Foundation (JQ201019)the Independent Innovation Foundation of Shandong University (2010JQ005 and 2012JC002).
文摘Hydrophobic fluorescence:Tan and his colleagues recently introduced a brand new chemotype of environment-sensitive fluorescent turn-on probes to detect the hydrophobic ligand-binding domain by using SBD fluorophore.The design strategy described in this report generalized the environment sensitivity turn-on mechanism to recognize a specific protein,which provides a robust breakthrough for interchanging fluorescence in conventional small-molecule fluorescent imaging.
