关于Cartan域上极值问题的注记

研究了Cartan域上的极值问题.建立Cartan域的单位球之间极值问题的一个定理并给出它的一个应用.     

渡槽整体结构环境激励模态试验

为获得渡槽整体结构动力特性,开展单向SIMO法、双向MIMO法环境激励模态试验,选用增强频域分解法识别纵向、横向、竖向、横竖双向模态参数.结果表明:2种方法识别出的模态大多数谱峰明显、识别效果较好;纵向模态以排架结构振动为主,槽身整体平动或转动或不动;前4阶横向模态以排架结构振动为主,槽身整体平动或转动或横摇,第5阶模...     

余因子系的等价定义与树形表示

利用图论的方法,讨论了余因子系的性质,分析了余因子系的等价定义,给出了几种重要的等价形式.并利用树的特殊结构,给出了余因子系的树形表示,为引入多项式系各种形式的结式矩阵做了理论准备.     

多波段线性调频傅里叶域锁模光电振荡器

提出了一种基于傅里叶域锁模光电振荡器（Fourier domain mode-locked optoelectronic oscillator,FDML OEO）的多波段可重构线性调频信号产生方案.在该方案中,由扫频多波长激光器、相位调制器和光陷波滤波器等构成FDML OEO的核心单元——快速扫频的多通带微波光子滤波器.将扫频多通带微波光子滤波器的扫频周期和FDML OEO的环腔延时同步,可实现傅里叶域锁模,从而在FDML OEO腔内自激振荡产生多波段线性调频微波信号.与传统的基于高速基带线性调频微波源的微波光子多波段线性调频信号产生方案相比,该方案结构简单,成本低,不需要借助外部的高速基带线性调频微波源.此外,FDML OEO所产生的多波段线性调频信号的带宽和中心频率均宽带可调.该新型多波段线性调频微波信号源在先进多波段雷达、多业务泛在接入无线通信等系统中具有良好的应用前景.     

L-fuzzy拓扑空间中的相对T3分离性

定义了L-fuzzy拓扑空间中的相对T1分离性和相对正则(T3)分离性,讨论了相对T1分离性和相对正则(T3)分离性的一系列性质.证明了相对正则分离性和相对T3分离性是相对闭遗传的,弱同胚不变的,L-好的推广性质,给出了相对T3分离性不是相对遗传的一个反例.     

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。     

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.     

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