基于芘希夫碱的汞离子荧光探针的合成与性能研究

以4-氯-7-硝基苯并呋咱（NBD-Cl）和芘甲醛为原料,设计合成了一种荧光化合物芘苯并呋咱类希夫碱,并通过核磁、质谱对其结构进行了表征. 结果表明：在二甲基亚砜（DMSO）水溶液中,该化合物能够对Hg2+表现出荧光增强响应,而相同条件下其他重金属离子对该化合物几乎没有类似的荧光识别现象. 因此,该荧光化合物对Hg2+具有专一荧光识别作用,是一种有效的Hg2+荧光探针.     

改良型9Cr-1Mo钢的形变热处理强化机制

采用形变热处理技术有效地提高改良型T91 耐热钢的高温回火抗力和室温综合力学性能。该钢经形变热处理后性能提高的主要机制是细晶强化和伴随晶粒细化而产生的马氏体组织的细化以及析出物的弥散分布。     

灰铸铁的应力屈服曲面及其三维热弹塑性应力解析

对原有的灰铸铁件应力屈服曲面进行了合理的简化,使其在理论上合理,工程应用上更为方便。建立了灰铸铁件三维非稳态热弹塑性应力场的有限元方法。以灰铸铁哑铃件为对象,用新屈服曲面对其应力发展过程进行了模拟,且比较了用新旧屈服面计算得到的结果。     

扩容图及其谱性质

目的 研究扩容图的若干性质.方法 用代数分析法研究图的结构.结果 利用图的剖分线图的结构,给出了新的广义线图,我们称之为扩容图.结论 讨论了扩容图的若干基本性质,给出了图与其扩容图参数之间的关系,并由此确定了扩客图谱性质.     

Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease

The AAA domain, a conserved Walker-type ATPase module, is a feature of members of the AAA family of proteins, which are involved in many cellular processes, including vesicular transport, organelle biogenesis, microtubule rearrangement and protein degradation. The function of the AAA domain, however, has not been explained. Membrane-anchored AAA proteases of prokaryotic and eukaryotic cells comprise a subfamily of AAA proteins that have metal-dependent peptidase activity and mediate the degradation of non-assembled membrane proteins. Inactivation of an orthologue of this protease family in humans causes neurodegeneration in hereditary spastic paraplegia. Here we investigate the AAA domain of the yeast protein Yme1, a subunit of the iota-AAA protease located in the inner membrane of mitochondria. We show that Yme1 senses the folding state of solvent-exposed domains and specifically degrades unfolded membrane proteins. Substrate recognition and binding are mediated by the amino-terminal region of the AAA domain. The purified AAA domain of Yme1 binds unfolded polypeptides and suppresses their aggregation. Our results indicate that the AAA domain of Ymel has a chaperone-like activity and suggest that the AAA domains of other AAA proteins may have a similar function.