中国八种家鼠C-带核型的比较研究

对我国大陆八种家鼠的C-带核型进行了比较研究, 并将C-带差异数量化 进 行模糊聚类分析 结果表明: 八种家鼠的C-带核型相互间存在一定的差异, 通过 分析, 得到了八种家鼠的聚 类分析分支图, 分为二大组: 斯氏家鼠和环齿鼠为 一组 其余种类为另一组。图版1图1表4参23

两种长臂猿染色体的C���和Ag-NORs的比较研究

白眉长臂猿和白颊长臂猿的染色体C���核型中除多数染色体有着丝点C���外,一些染色体上还出现插入C���和着丝点C���弱化或减少现象;白眉长臂猿有全异染色质臂;白颊长臂猿有较多的端位C���。白眉长臂猿有两个Ag-NORs,而白颊长臂猿的Ag-NORs雌体有4个,雄体有5个,Y染色体上有NOR。

p53蛋白质C���的三维结构及生物功能区

利用p53 C���118个氨基酸的mRNA二级结构和Chou-Fasman蛋白质二级结构预测原则,预测p53蛋白质C���289-325为卷曲肽段,368-393段包括两段螺旋结构:#alpha#_(1)368-373、#alpha#_(2)381-388。其中三段已知的蛋白质二级结构与此mRNA二级结构单元间有准确的对应关系。与四种以多重序列联配为基础的蛋白质二级结构预测方法(准确率均为73.20%左右)相对照,预测结果基本一致。结合单体聚合区31个氨基酸晶体结构,在SGI INDIGO~(2)工作站上构建了p53 C���108个残基的三维结构。进一步揭示了p53 C���诸多生物功能区之间的空间构象关系。

The three dimensional structure and biological domains of the p53 C-terminus.

It was expected that there are a coil (289 similar to 325) and two a helix (alpha(1)368 similar to 373, alpha(2)381 similar to 388) structures in p53 protein C-terminal region based on its mRNA secondary structure template and Chou-Fasman's protein secondary structure principle of prediction. The result was conformed by the other four methods of protein secondary structure prediction that are based on the multiple sequence alignment (accuracy = 73.20%). Combine with the 31 amino acids crystal structure of the oligomerization, the three dimensional conformation of p53 C-terminal 108 residues was built using the SGI INDIGO(2) computer. This structure further expounds the relationship among those biological function domains of p53 C- terminus at three-dimensional level.

Molecular modeling on some human interleukins sharing gamma c of interleukin-2 receptor, and structure-function relationships

Five models for human interleukin-7 (HIL-7), HIL-9, HIL-13, HIL-15 and HIL-17 have been generated by SYBYL software package. The primary models were optimized using molecular dynamics and molecular mechanics methods. The final models were optimized using a steepest descent algorithm and a subsequent conjugate gradient method. The complexes with these interleukins and the common gamma chain of interleukin-2 receptor (IL-2R) were constructed and subjected to energy minimization. We found residues, such as Gln127 and Tyr103, of the common gamma chain of IL-2R are very important. Other residues, e.g. Lys70, Asn128 and Glu162, are also significant. Four hydrophobic grooves and two hydrophilic sites converge at the active site triad of the gamma chain. The binding sites of these interleukins interaction with the common gamma chain exist in the first helical and/or the fourth helical domains. Therefore, we conclude that these interleukins binds to the common gamma chain of IL-2R by the first and the fourth helix domain. Especially at the binding sites of some residues (lysine, arginine, asparagine, glutamic acid and aspartic acid), with a discontinuous region of the common gamma chain of IL-2R, termed the interleukins binding sites (103-210). The study of these sites can be important for the development of new drugs. (C) 2000 Elsevier Science B.V. All rights reserved.