随机变幅加载下疲劳强度可靠性分析

目前的疲劳强度及其概率分布是根据等幅Ｐ－Ｓ－Ｎ曲线族求得的，只能用于等幅加载，不能用于变幅及随机加载，而等效应力法又是根据常规ＭＩＮＥＲ准则进行转换的，无法用于可靠性分析，本文首次明确提出等幅疲劳强度，变幅疲劳强度及随机加载疲劳强度的概念，并且运用二维概率ＭＩＮＥＲ法则，通过建立变幅及随机加载的Ｐ－Ｓａ－Ｓｍ－Ｎｖ曲面族方程，提出了变幅及随机加载下疲劳强度可靠性分析的一套系统方法，具有重要的工程尖     

沸石分子筛材料中次级孔的研究——Ⅱ.Y型沸石晶内次级孔对扩散的影响

以含有次级孔的沸石的晶内扩散为研究对象,对来源于同一NaY母体的一组改性Y型沸石,进行了孔结构分析和正戊烷的扩散系数的测定。得到了具不同次级孔量的Y型沸石晶内扩散性能变化的规律。并采用随机游动方法对实际的Y型沸石晶内扩散进行模拟,得到了与实验测定一致的结果,从而可以对有次级孔的Y型沸石的晶内扩散做定量的估计。     

优化技术用于交错管道双环连接设计

对双环管连接交错管道问题,从几何分析到目标函数的建立,加上各种约束条件,通过计算机运算,非常迅速、有效地求得各项设计参数,从而满足工程的各种需要。     

独立随机变量第k个最大值的密度函数的局部一致收敛

ξ_1,ξ_2,…,ξ_n是独立同分布随机变量,公共分布函数F(x)绝对连续,g_n.k(x)为ξ_1,…,ξ_n的第k个规范化最大值的分布密度函数.本文讨论了g_n,k(x)的局部一致收敛性以及在L_p(O相似文献   

随机变量的函数相关性

引入了“曲线分布密度函数”的定义;给出了由边缘密度及两个随机变量间的函数式表示曲线分布的解析表达式;研究了曲线分布密度的简单性质及由它求两个随机变量间的函数式和边缘密度的公式;对有一般函数关系的两个随机变量,推导出条件分布函数、条件分布列及条件数学期望的分析式。     

基于马尔可夫随机场的遥感图像分割和描述

讨论了基于马尔可夫随机场的遥感图像分割．根据卫星遥感图像的特点,建立了相应的基于马尔可夫随机场的图像分割模型．由此将图像分割问题转化成图像标记问题, 并进一步转化成求图像的最大后验概率估计的问题． 本文引进了一种基于博弈理论的决定性退火算法, 可以用该算法对图像进行标记, 该算法收敛于局部最大, 在实验中取得了很好的效果．     

Louis H．Y．Chen定理的推广

ＬｏｕｔｓＨ．Ｙ．Ｃｈｅｎ在文［１］中应用测度论的方法，证明标准正态随机向量的一个充分条件．本文指出它也是必要条件．同时将它推广到一般多元正态分布的情形，从而得到几个一般性结论．     

Integrating Multi-Source Web Records into Relational Database

How to integrate heterogeneous semi-structured Web records into relational database is an important and challengeable research topic. An improved model of conditional random fields was presented to combine the learning of labeled samples and unlabeled database records in order to reduce the dependence on tediously hand-labeled training data. The pro- posed model was used to solve the problem of schema matching between data source schema and database schema. Experimental results using a large number of Web pages from diverse domains show the novel approach＇s effectiveness.     

Protein folding revisited. A polypeptide chain at the folding – misfolding – nonfolding cross-roads: which way to go?

The structure-function paradigm claims that a specific function of a protein is determined by its unique and rigid three-dimensional (3D) structure. Thus, following its biosynthesis on the ribosome, a protein must fold to be functional. This idea represents one of the cornerstones of modern biology. Numerous cases when, due to the effect of environmental factors or because of genetic defects (mutations), a polypeptide chain has lost its capability to gain a proper functional 3D structure (i.e. became misfolded), seem to confirm this concept. Consequences of such misfolding are well known and represent lost of function, aggregation, development of conformational disorders and cell death. However, the recent revelation of countless examples of intrinsically disordered proteins has cast doubt on the general validity of the structure-function paradigm and revealed an intriguing route of functional disorder. Thus, in a living cell, a polypeptide chain chooses between three potential fates – functional folding, potentially deadly misfolding and mysterious nonfolding. This choice is dictated by the peculiarities of amino acid sequence and/or by the pressure of environmental factors. The aim of the present review is to outline some interesting features of these three routes.Received 5 March 2003; received after revision 28 March 2003; accepted 31 March 2003