上三角矩阵代数上的保不变子空间格映射

设Tn是数域F上的n×n阶上三角矩阵代数,其中F是实数域R或复数域C.利用矩阵的可加性,证明了Tn上的每一个保不变子空间格的可加映射Φ为:Φ(A)=αA+φ(A)I ((A)A∈Tn),其中α是非零常数,φ∶Tn←F是可加映射,I∈Tn是单位算子.     

基于三角模糊数的汉服袖型感性评价北大核心CSCD

为探究消费者对汉服袖型的感性认知,帮助服装设计师更准确地把握消费者心理,文章选取具有代表性的8款汉服袖型,采用语意差异法收集袖型样本在6对感性形容词汇上的感性评价,将其用三角模糊数的形式进行表征,并对模糊评价结果的准确性进行检验。为得到各汉服袖型较为精确的感性评价,文章对三角模糊数进行贴近度分析,并将贴近度的结果作为依据,运用系统聚类的方法将汉服袖型分为4类。研究表明:各汉服袖型因袖宽大小、袖缘线条形状、袖长、袖口形状的不同,感性评价存在一定差异,且最终感性评价结果符合客观认知。经验证可知,利用三角模糊数能够较准确地对汉服袖型进行感性评价。     

三角代数上的n阶导子系

设U=Tri(A,M,B)是三角代数,Dn={δ0,δ1,…,δn}为U上的一组可加映射且δ0=I.若A,B∈U有δm(AB)=∑mk=0Cmkδk(A)δm-k(B)(m=0,1,2,…,n),则称Dn为U上的一个n阶导子系,若A∈U有δm(A2)=∑mk=0Cmkδk(A)δm-k(A)(m=0,1,2,…,n),则称Dn为U上的一个n阶Jordan导子系.利用算子论的方法讨论了三角代数上的n阶导子系,证明了三角代数上的每个n阶Jordan导子系都是n阶导子系.     

RoCoS紧密纺纱新技术

文章介绍了一种新的紧密纺纱技术--RoCoS(Rotorcraft Compact Spinning System).RoCoS紧密纺纱系统借助于RoCoS组合件构成三罗拉四皮辊牵伸结构,采用磁铁--机械式原理集束,相继实现纱线的牵伸、集聚和加捻.RoCoS紧密纺纱技术结构简单,安装便捷,使用可靠,维护方便,克服了传统气流集束式紧密纺技术的不足.它适于纺棉型或毛型纱线,可用于新机或老机改造,是一种有较强市场发展潜力的新型紧密纺纱技术.     

三角代数上的ξ-Lie可导映射

设U=Tri(A,M,B)是含单位元I的三角代数并且φ:U→U是线性映射.利用代数分解的方法,证明了当三角代数U满足适当条件时,如果U,V∈U且UV=VU=I,有φ([U,V]ξ)=[φ(U),V]ξ+[U,φ(V)]ξ(ξ≠±1),则φ是导子.并得到了套代数上ξ-Lie可导映射的一个刻画.     

Molecular Characterization and Expression Pattern of Tripartite Motif Protein 39 in Gallus gallus with a Complete PRY/SPRY Domain

Members of tripartite motif (TRIM) proteins in mammals play important roles in multiple cellular processes in the immune system. In the present study we have obtained the chicken TRIM39 with the insertion of a base A at position 1006 bp, compared to the sequence in the NCBI database (Accession No: NM 001006196), which made TRIM39 fulfill the TRIM rule of domain composition with both PRY, and SPRY domains. The open reading frame consisted of 1392 bp encoding 463 amino acid residues. The amino acid sequences of TRIM39 protein in mammals were highly similar (from 91.48% to 99.61%), while chicken TRIM39 had relatively low homology with mammals (from 29.2% to 39.59%). Real time RT-PCR indicated that the mRNA expression level of TRIM39 was the highest in spleen, with a lower expression in liver, brain, and lung, suggesting it might be an important protein participating in the immune system.     

Crystal structure of the bacterial ribosomal decoding site complexed with a synthetic doubly functionalized paromomycin derivative: a new specific binding mode to an a-minor motif enhances in vitro antibacterial activity

The crystal structure of the complex between oligonucleotide containing the bacterial ribosomal decoding site (A site) and the synthetic paromomycin analogue 1, which contains the gamma-amino-alpha-hydroxybutyryl (L-haba) group at position N1 of ring II (2-DOS ring), and an ether chain with an O-phenethylaminoethyl group at position C2' of ring III, is reported. Interestingly, next to the paromomycin analogue 1 specifically bound to the A site, a second molecule of 1 with a different conformation is observed at the crystal packing interface which mimics the A-minor interaction between two bulged-out adenines from the A site and the codon-anticodon stem of the mRNA-tRNA complex. Improved antibacterial activity supports the conclusion that analogue 1 might affect protein synthesis on the ribosome in two different ways: 1) specific binding to the A site forces maintenance of the "on" state with two bulged out adenines, and 2) a new binding mode of 1 to an A-minor motif which stabilizes complex formation between the ribosome and the mRNA-tRNA complex regardless of whether the codon-anticodon stem is of the cognate or near-cognate type.     

Prediction of a New Ligand-Binding Site for Type 2 Motif based on the Crystal Structure of ALG-2 by Dry and Wet Approaches

ALG-2 is a penta-EF-hand Ca(2+)-binding protein and interacts with a variety of intracellular proteins. Two types of ALG-2-binding motifs have been determined: type 1, PXYPXnYP (X, variable; n = 4), in ALIX and PLSCR3; type 2, PXPGF, in Sec31A and PLSCR3. The previously solved X-ray crystal structure of the complex between ALG-2 and an ALIX peptide containing type 1 motif showed that the peptide binds to Pocket 1 and Pocket 2. Co-crystallization of ALG-2 and type 2 motif-containing peptides has not been successful. To gain insights into the molecular basis of type 2 motif recognition, we searched for a new hydrophobic cavity by computational algorithms using MetaPocket 2.0 based on 3D structures of ALG-2. The predicted hydrophobic pocket designated Pocket 3 fits with N-acetyl-ProAlaProGlyPhe-amide, a virtual penta-peptide derived from one of the two types of ALG-2-binding sites in PLSCR3 (type 2 motif), using the molecular docking software AutoDock Vina. We investigated effects of amino acid substitutions of the predicted binding sites on binding abilities by pulldown assays using glutathione-S-transferase -fused ALG-2 of wild-type and mutant proteins and lysates of cells expressing green fluorescent protein -fused PLSCR3 of wild-type and mutants. Substitution of either L52 with Ala or F148 with Ser of ALG-2 caused loss of binding abilities to PLSCR3 lacking type 1 motif but retained those to PLSCR3 lacking type 2 motif, strongly supporting the hypothesis that Pocket 3 is the binding site for type 2 motif.     

The A9 Core Sequence from NRPS Adenylation Domain Is Relevant for Thioester Formation

The adenylation (A) domain in nonribosomal peptide synthetases catalyses a two-step reaction in which an amino acid is activated and then transferred to the neighbouring thiolation (T) domain. In this study, we investigated the role of the conserved A9 core sequence of the A-domain of tyrocidine synthetase 1, by analysis of single amino acid mutations in the A9 region. Mutation of an absolutely conserved proline (P490G) significantly reduced the conformational stability of the protein, as evidenced by increased susceptibility to proteolytic cleavage and denaturation. All mutant A-domains were capable of amino acid activation, but the activity in the overall reaction was reduced. Surprisingly, the S491R mutant (mutation at the first residue following the A9 motif) showed elevated overall activity compared to the wild-type protein. Our results suggest that the A9 core sequence plays a role in the second reaction step, in which it could serve as a "clip" for the proper positioning of residues important for the interaction with the T-domain, and/or stabilisation of the thioester-forming conformation.