Balcha opaca Fusu sp. n. (Insecta: Hymenoptera): availability of the species name

ABSTRACT

The purpose of this paper is to describe the circumstances of publication of an unavailable name of chalcid wasps, and to make the name Balcha opaca Fusu sp. n. (Hymenoptera: Eupelmidae) available.

www.zoobank.org/urn:lsid:zoobank.org:pub:38F49D79-F5AA-4516-8E48-55CFFA61A71C     

一种基于动态服务规格的病态流控制方法

在区分服务网络确保转发(assured forwarding)服务中,提出一种基于动态服务规格(service profiles)的病态流控制机制。该机制在DS域的入口节点(ingress node)根据核心节点反馈的信息动态地调整病态流的当前服务规格和进入DS域的速率,达到控制病态流的目的。模拟实验表明,该机制可以有效地提高正常业务流的性能,控制由病态流引起的DS域内全局最大-最小不公平(global max-min unfairness)问题。     

基于图论的平面机械系统仿真

在简要介绍了图论的基本思想和方法之后,具体阐述了如何运用图论结合矢量力学的方法来建立机械系统的数学模型,并举例说明了普通三维系统数学模型的建立过程。运用该方法编写了仿真软件VECDYNA,并用其对双杆复摆系统和曲柄滑块系统分别进行了仿真分析。并将其结果与ADAMS的仿真结果进行了对比,对仿真结果进行了验证。结果表明基于图论的多体动力学研究是研究机械系统仿真的一种有效、节省资源的方法。     

倾斜转弯导弹三回路鲁棒自动驾驶仪设计

针对倾斜转弯导弹,提出了最优/经典综合设计方法设计自动驾驶仪.该方法应用最优控制设计出俯仰/偏航混合通道三回路自动驾驶仪,设计中同时对开环系统的奇异值频域曲线进行约束,以保证系统具有一定的鲁棒性,获得的三回路自动驾驶仪结构简单,易于工程实现.仿真结果证实了其具有良好的跟踪性能和鲁棒性,也表明该自动驾驶仪能满足倾斜转弯导弹协调倾斜转弯的要求.     

弹载消旋平台双模控制与仿真研究

为了消除弹体转动对惯性平台及天线运动耦合的影响,设计了旋转导弹消旋平台,并将模糊控制器与常规PID相结合,建立消旋平台Fuzzy-PID双模控制仿真模型。采用MATlAB和MATlAB/ADAMS联合仿真方法对消旋平台双模控制系统进行仿真分析。结果表明,Fuzzy-PID双模控制使惯性平台及天线的稳态性能得到明显改善。     

N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism

MurNAc etherases cleave the uniqued-lactyl ether bond of the bacterial cell wall sugar N-acetylmuramic acid (MurNAc). Members of this newly discovered family of enzymes are widely distributed among bacteria and are required to utilize peptidoglycan fragments obtained either from the environment or from the endogenous cell wall (i.e., recycling). MurNAc etherases are strictly dependent on the substrate MurNAc possessing a free reducing end and a phosphoryl group at C6. They carry a single conserved sugar phosphate isomerase/sugar phosphate- binding (SIS) domain to which MurNAc 6-phosphate is bound. Two subunits form an enzymatically active homodimer that structurally resembles the isomerase module of the double-SIS domain protein GlmS, the glucosamine 6-phosphate synthase. Structural comparison provides insights into the two-step lyase-type reaction mechanism of MurNAc etherases: β-elimination of the D-lactic acid substituent proceeds through a 2,3-unsaturated sugar intermediate to which water is subsequently added. Received 31 August 2007; received after revision 12 October 2007; accepted 1 November 2007     

Starch-binding domains in the post-genome era

Starch belongs to the most abundant biopolymers on Earth. As a source of energy, starch is degraded by a large number of various amylolytic enzymes. However, only about 10% of them are capable of binding and degrading raw starch. These enzymes usually possess a distinct sequence-structural module, the so-called starchbinding domain (SBD). In general, all carbohydrate-binding modules (CBMs) have been classified into the CBM families. In this sequence-based classification the individual types of SBDs have been placed into seven CBM families: CBM20, CBM21, CBM25, CBM26, CBM34, CBM41 and CBM45. The family CBM20, known also as a classical C-terminal SBD of microbial amylases, is the most thoroughly studied. The three-dimensional structures have already been determined by X-ray crystallography or nuclear magnetic resonance for SBDs from five CBM families (20, 25, 26, 34 and 41), and the structure of the CBM21 has been modelled. Despite differences among the amino acid sequences, the fold of a distorted β-barrel seems to be conserved together with a similar way of substrate binding (mainly stacking interactions between aromatic residues and glucose rings). SBDs have recently been discovered in many non-amylolytic proteins. These may, for example, have regulatory functions in starch metabolism in plants or glycogen metabolism in mammals. SBDs have also found practical uses. Received 25 May 2006; received after revision 26 June 2006; accepted 3 August 2006     

SET domain protein lysine methyltransferases: Structure, specificity and catalysis

Site- and state-specific lysine methylation of histones is catalyzed by a family of proteins that contain the evolutionarily conserved SET domain and plays a fundamental role in epigenetic regulation of gene activation and silencing in all eukaryotes. The recently determined three-dimensional structures of the SET domains from chromosomal proteins reveal that the core SET domain structure contains a two-domain architecture, consisting of a conserved anti-parallel β-barrel and a structurally variable insert that surround a unusual knot-like structure that comprises the enzyme active site. These structures of the SET domains, either in the free state or when bound to cofactor S-adenosyl-L-homocysteine and/or histone peptide, mimicking an enzyme/cofactor/substrate complex, further yield the structural insights into the molecular basis of the substrate specificity, methylation multiplicity and the catalytic mechanism of histone lysine methylation. Received 10 June 2006; accepted 22 August 2006     

Optimization of the cellular import of functionally active SH2-domain-interacting phosphopeptides

Phosphopeptides interacting with src homology 2 (SH2) domains can activate essential signaling enzymes in vitro. When delivered to cells, they may disrupt protein-protein interactions, thereby influencing intracellular signaling. We showed earlier that phosphopeptides corresponding to the inhibitory motif of Fcγ receptor IIb and a motif of the Grb2-associated binder 1 adaptor protein activate SH2-containing tyrosine phosphatase 2 in vitro. To study the ex vivo effects of these peptides, we have now compared different methods for peptide delivery: (i) permeabilization of the target cells and (ii) the use of cell-permeable vectors, which are potentially able to transport biologically active compounds into B cells. We found octanoyl-Arg₈ to be an optimal carrier for the delivery of phosphopeptides to the cells. With this strategy, the function of cell-permeable SHP-2-binding phosphopeptides was analyzed. These peptides modulated the protein phosphorylation in B cells in a dose- and time-dependent manner. Received 27 July 2006; received after revision 4 September 2006; accepted 18 September 2006     

领域本体信息源选取方法研究与实现

构造领域本体所需的信息源选取方法的研究对解决本体的构造质量、构造效率等问题,以及推广与发展领域本体有着重要意义.传统的信息源文档选取方法只考虑概念因素,不能很好地解决该问题.因此,首先利用抽象方法分析了领域本体所需信息源具有的概念性、关系性和预测性等特点.然后,针对这些特点分别采用改进的VSM方法、基于本体关系距离的方法以及神经网络方法计算文档权值.最后,通过编写的软件OnMaker产生模拟数据得到概念、关系和预测3个权值,从而计算出每个文档权值,并使用与"湿地保护"相关的真实文档验证该模型,达到了较好排序选取的效果.