Frenkel-Kontorova Model with Alternant Coupling Potential

We have studied a modified Frenkel-Kontorova (FK) model with alternant coupling potential. From it, we obtain a coupling conservative map, it shows that the gold-mean number is not the last broken winding number, and the broken critical value is varied with the variance of strength of spire. The phase diagram becomes asymmetric in a period. The Devil's staircase and generalized dimension are different from those of the standard FK model.PACS numbers: 64.60.Fr, 05.70.Fh, 05.70.Jk     

环戊烯分子内价轨道1a′的电子动量谱学研究

报道了环戊烯（C₅H₈）分子1a′轨道的电子动量谱，并且给出了价 轨道的电离能谱信息 .实验在非共面对称几何条件下用能量多道型电子动量谱仪完成，入射电子的能量为1200 eV 加结合能.通过Hartree-Fock 和密度泛函方法计算得到了C₅H₈分子 1a′轨道的动量谱. 对1a′轨道的电子动量谱的实验值和理论计算进行了比较，得到了该轨道的极强度（pole s trength）的信息.     

利用光生物传感器研究阳离子卟啉与人血清白蛋白的相互作用

An optical biosensor with a stirred cuvette has been used to monitor the interaction between immobilized human serum albumin （HSA） and three water-soluble cationic porphyrins. The binding constants at 25℃ obtained from biosensor analysis were compared with those from fluorescence spectroscopy. The interactions were further investigated at temperatures from 15℃ to 30℃. The thermodynamics parameters, changes of free energy （△G）, enthalpy （△H） and entropy （△S）, were evaluated from equilibrium data. It appeared that the binding process was governed primarily by electrostatic forces.     

pH Induces Thermal Unfolding of UTI: An Implication of Reversible and Irreversible Mechanism Based on the Analysis of Thermal Stability, Thermodynamic, Conformational Characterization

The thermal unfolding of Urinary Trypsin Inhibitor (UTI) was studied by several methods: Circular Dichroism (CD), Fluorescence and UV–Vis spectra. Thermal melting of UTI, dissolved in the neutral and basic buffers, was proved to be irreversible and two domains of UTI unfolded simultaneously, but the melting was reversible and the intermediate was observed when pH is lower than 4.2. The result suggested that heat and changes in pH, which had a more important impact on the stabilization of the domain I and the interaction between two domains, might cause different unfolding transitions. A reasonable explanation was deduced for the mechanism of reversible and irreversible thermal unfolding based on the effect of pH on the protein structure, the analysis of thermal transitions and the result of Electron Microscopy: In neutral and basic buffers, the Reactive Central Loop (RCL) in domain II can interact with or insert into the partial expanding domain I and UTI become self-polymerization, however, no aggregation can be observed in acid buffer since low pH and heat destabilized the structure of the domain I and the native conformation can restructure. The interaction between the special structural element RCL and domain I play an important role in the formation of polymer which was different from other two reasons given by other authors—the cleavage of disulfide and the formation of irregular polymer mainly based on hydrophobic interaction.     

Optimality of E-pseudoconvex multi-objective programming problems without constraint qualifications

In this note, we consider the optimality criteria of multi-objective programming problems without constraint qualifications involving generalized convexity. Under the E-pseudoconvexity assumptions, the unified necessary and sufficient optimality conditions are established for weakly efficient and efficient solutions, respectively, in multi-objective programming problems.