链球菌G蛋白的力致去折叠研究

G蛋白是一个小蛋白,且是研究蛋白质去折叠的理想模板。当使用机械力对其进行拉伸研究时,发现G蛋白的去折叠过程中存在明显的中间态。在恒力和恒速两种情况下进行拉伸分子动力学模拟,发现其在两种情况下具有相同的去折叠次序,即是C端的β片层部分先去折叠,接着是N端的β片层部分去折叠,然后是C端的β片层完全去折叠,最后是N端的β片层完全去折叠,研究表明氢键对其去折叠有着重要的作用。通过研究对进一步认识蛋白质去折叠机制有重要的参考价值。     

Cause of Irreversible Inactivation of Aminoacylase in Urea Solution

ＩｎｔｒｏｄｕｃｔｉｏｎＡｍｉｎｏａｃｙｌａｓｅ (Ｎ ａｃｙｌａｍｉｎｏａｃｉｄａｍｉｄｏｈｙｄｒｏｌａｓｅ .ＥＣ 3.5.1.14 ) ,ｗｈｉｃｈｅｘｉｓｔｓｉｎｍａｍｍａｌｉａｎｋｉｄｎｅｙｓａｎｄｍｉｃｒｏｏｒｇａｎｉｓｍｓ ,ｃａｔａｌｙｚｅｓｔｈｅｒｅｖｅｒｓｉｂｌｅｈｙｄｒｏｌｙｓｉｓｏｆＬ ａｃｙｌａｍｉｎｏａｃｉｄｓ[1] .Ｔｈｅｅｎｚｙｍｅｉｓｄｉｍｅｒｉｃｗｉｔｈａｒｅｌａｔｉｖｅｍｏｌｅｃｕｌａｒｗａｓｓｏｆ86 0 0 0 ,ｃｏｎｔａｉｎｉｎｇｏｎｅＺｎ2 ｉｏｎｐｅｒｓｕｂｕｎｉｔｗｈｉｃｈｉｓ…     

高质量圆和椭圆曲线在计算机图形输出中快速生成的算法研究

本文给出一个以等分角度为增量的绘制和椭圆曲线的算法。以计算圆为基础，构造的表达式直接对ｓｉｎθ和ｃｏｓθ的泰勒展开式进行，计算精度较高，同时也减少了计算量。     

Graded stable unfoldings in bifurcation problems

We introduced stability of arbitrary degree number for unfordings of bifurcation problems and established the equivalence of three stabilities. Thom's transversality theory is used to character the new stability. Foundation item: Supported by the National Natural Science Foundation of China (19871074) Biography: Zhang Guo-bin (1939-), male, Professor, research interest: singularity theory.     

含两组状态变量的等变分歧问题在A（Г）的一个子群下的通用开折

基于奇点理论中光滑映射芽的左右等价关系，得到了在左右等价群A（Г）的一个子群作用下，含两组状态变量的多参数等变问题的开折是通用开折的充要条件。     

Hopf分岔的万有普适开折的代数条件

对经Lyapunov-Schmidt约化后所得分岔方程强Z2等价于某三个正规形的Hopf分岔问题给出了求解万有普适开折问题的代数条件。     

Unfolding and Inactivation of Green Crab ( Scylla Serrata) Alkaline Phosphatase during Thermal Denaturation *

ＩｎｔｒｏｄｕｃｔｉｏｎＴｈａｔｉｎａｃｔｉｖａｔｉｏｎｏｃｃｕｒｓｂｅｆｏｒｅｎｏｔｉｃｅａｂｌｅｃｏｎｆｏｒｍａｔｉｏｎａｌｃｈａｎｇｅｓｃａｎｂｅｄｅｔｅｃｔｅｄｄｕｒｉｎｇｄｅｎａｔｕｒａｔｉｏｎｏｆｃｒｅａｔｉｎｅｋｉｎａｓｅａｎｄｏｔｈｅ...     

Aviko K型钢球外观检验机中子午线展开机构的理论分析

对Ａｖｉｋｏ Ｋ型钢球外观检验机中独特的钢球子午线展开机构进行理论分析，将单驱动轮展开机构与双驱动轮展开机构了比较。推导出用于加工该展开机构的易损件－控制滚轮几何加工参数的计算公式。利用该理论分析结果设计出的控制滚轮加工、研磨设备，目前已成功地得到应用。     

一类高余维静态分岔问题分析

分析了一种特殊的分岔，讨论了它的范式和普适开折问题。对Z2对称情况，给出了普适开折和相应分岔图。因在开折参数不等于0时，其分岔图分别具有树枝分岔和简单分岔的特征，将该分岔点为半树枝／半简单分岔点。对Z2对称性破缺的情况，利用奇异性理论，导出了余维数为5的普适开折的所有4种形式，并结合具体的应用给出了其部分分岔图。     

Unfolding of C2A Domain of Synaptotagmin I in the Presence of Guanidine Hydrochloride

The C2 domain originally referred to the second of four constant structural motifs in protein kinase C (PKC). Now this domain represents a large structural family sharing a homologous dimensional structure in many proteins that play important roles in many organisms. The C2A domain is one of the two C2 domains of synaptotagmin I involved in the Ca^2 regulation of exocytosis. This domain is mostly composed of β-sheet except for a small fraction of α-helix, and therefore provides an ideal model for a protein folding study. In this report, the unfolding equilibrium of the C2A domain in guanidine hydrochloride (GdnHCI) containing solutions has been studied using ultraviolet (UV) difference spectrum, fluorescence spectrum, size exclusion chromatography (SEC), and circular dichroism (CD) spectrum. The results suggest that unfolding of the C2A domain occurs as a two-state process during GdnHCI titration. By examining the changes of both tertiary structure and secondary structure, no intermediates could be detected during this unfolding study. However, it has been found that the native state of the C2A domain has a large hydrophobic surface. This result suggests that as a fragment of a protein, the C2A domain itself may exist in a state with large hydrophobic surface. This hydrophobic surface may be the molecular basis for interaction between domains in the whole protein.Furthermore, the hydrophobic behavior may play a role during the oligomerization of svnaptotagmin.