基于ANSYS的闩体刚强度有限元分析

闩体的刚度和强度必须满足设计要求。用有限元法对复杂结构件进行力学性能分析是非常有效的方法。采用ANSYS软件对闩体进行了刚度和强度分析,得出了有用的结论,可供相关设计借鉴。     

Specifying transformer winter and summer peak-load limits

This paper presents a methodology for specifying the winter and summer peak-load limits for substation transformers that carry a temperature-sensitive load, taking into account the random nature of load and ambient temperature as well as their correlation. With this methodology, we can easily and accurately specify the peak-load limits for each substation transformer once the historical ambient temperature and load data are available. Also, we can collectively specify the peak-load limits for the transformer of each cooling type (OA, OA/FA, or OA/FA/FA) in a geographic region based on the mean and standard deviation of ambient temperatures in that region. Such peak-load limits are useful for power system planning.     

模糊技术的发展及在相关领域中的应用

本文介绍了模糊技术的发展和现状，以及在相关领域中的应用情况，并且讨论了模糊技术在我国的产业化方向等问题。     

As,Sb,Sn对30CrMnSiA钢力学性能的影响

在３０ＣｒＭｎＳｉＡ钢中加入不同量的Ａｓ，Ｓｂ，Ｓｎ元素，研究了这些元素单独存在及复合存在时对钢的强度，塑性，冲击韧度及韧脆转变温度的影响规律，并用扫描电镜及俄歇能谱分析了Ａｓ，Ｓｂ，Ｓｎ导致晶界脆化的机理。     

用EGS4分析9MeV行波直线加速器屏蔽系统

采用了国际上广泛使用的ＭｏｎｔｅＣａｒｌｏ模拟计算程序ＥＧＳ４对海关集装箱检测系统用加速器屏蔽系统进行了辐射模拟分析，与实际测试数据进行分析、比较，解释了特殊剂量分布的原因，提出了系统改进的参考方案。     

A simplified dispersion limit formula for IM/DD systems and itscomparison with experimental results

A simplified formula for the dispersion limit of single-mode-fiber intensity modulation/direct detection (IM/DD) systems is derived for arbitrary given normalized pulse width U, eye opening penalty X and source linewidth enhancement factor α. From the comparison with published theoretical analyses, computer simulation and experimental data, its validity and the limits of existing formulae are shown. Using this simple and general formula, one can easily obtain the dispersion limit of various fiber types under different working conditions in IM/DD systems     

γ 射线引发 VAc 乳液聚合以制备白乳胶的动力学及工艺条件研究

研究了ＶＡｃ的辐射乳液聚合动力学，并对其聚合工艺条件作了初步探索。得出ＶＡｃ乳液在进行辐射聚合时，成核期结束较早（转化率在１０％以下），有相当长的恒速期存在。乳胶粒子直径在０．５～３μｍ之间，比一般的乳液聚合乳胶粒子要大。同时从动力学数据还可以看出几种成核机理（胶束成核，水相成核和液滴成核）同时存在，由此对试验条件提出了相应的要求。     

Conformational stability of factor VIIa: biophysical studies of thermal and guanidine hydrochloride-induced denaturation

The binding of the multidomain protein factor VIIa (fVIIa) to tissue factor provides the interprotein communication necessary to make fVIIa an efficient catalyst of the initial event in the extrinsic pathway of blood coagulation. We have investigated the stability of individual domains in fVIIa and the influence of Ca2+ and an irreversible active-site inhibitor (FFR-chloromethyl ketone). Equilibrium guanidine hydrochloride (GuHCl)-induced unfolding monitored by tryptophan fluorescence and far-UV circular dichroism (CD) demonstrated that the gamma-carboxyglutamic acid (Gla) domain unfolds at 0.3 M GuHCl and the serine protease (SP) domain at 3 M GuHCl and that Ca2+ is a prerequisite for the formation of an ordered, compact structure in the Gla domain. The loss of amidolytic activity coincides with the first transition, which is stabilized by the active-site inhibitor, and a change in the environment of the active site is demonstrated using a fluorescent inhibitor (DEGR-chloromethyl ketone). Thermal unfolding monitored by differential scanning calorimetry (DSC) reveals that Ca2+ stabilizes the SP domain slightly, increasing the unfolding temperature by 2.7 degrees C. In addition, Ca2+ is required for a large enthalpy change concomitant with unfolding of the Gla domain, and this unfolding enthalpy is only detectable in the presence of the SP domain, indicating some kind of interaction between these domains. Thermal unfolding measured by CD indicates secondary structural changes at the same temperature as the heat absorption in the DSC but only when both the Gla domain and the SP domain are present together with Ca2+ ions. Taken together, these results indicate a Ca2+-dependent interaction between the Gla domain and the SP domain, implying a high degree of flexibility of the domains in free fVIIa. It is also shown that the epidermal growth factor-like domains are stable at elevated temperatures and high GuHCl concentrations. Moreover, already at physiological temperature, subtle structural changes take place which influence the overall shape of fVIIa and are detrimental to its enzymatic activity.