多元超立方体交换结构信元丢失率仿真分析

研究了多元超立方体交换结构(MHSF)的信元丢失率性能。分析表明，当各交换节点的流量均匀地发送到各个目的节点时，MHSF的信元丢失率d与MHSF的元数k、链路加速因子s、链路缓冲大小m以及节点内部端口数M等因素有关；同时仿真结果显示，在可应用参数范围内，d明显有随着s、m或k(通常M固定)的增加呈指数规律下降的趋势，并且在较小参数条件下MHSF就具有较低的信元丢失率。     

Logistic脉冲系统的最优脉冲控制

利用脉冲微分方程的周期性理论和最优控制原理,研究了Logistic周期脉冲系统的最优脉冲控制,给出了所研究系统的最佳控制周期和相应的最优捕获量.     

激光测距仪使用中的几个问题

在外业工作中,因国产激光测距仪时有故障发生而影响其广泛使用。本文以HQ-102型激光测距陡为例,简述其在使用中常出现的频率漂移、锁相电路失锁、内检棱镜移位等故障及排除方法。     

中性载体DAM推动Ca^2＋离子在水／硝基苯界面的转移

本文用卷积(半微分和半积分)循环伏安法研究了中性载体DAM(二安替比林甲烷)络合推动Ca~(2 )离子在水/硝基苯界面的转移过程,探讨了有关转移过程的机理,测定了相应的扩散系数和配合物的络合稳定常数。     

Poly(ADP-ribose) is required for spindle assembly and structure

The mitotic spindle is typically thought of as an array of microtubules, microtubule-associated proteins and motors that self-organizes to align and segregate chromosomes. The major spindle components consist of proteins and DNA, the primary structural elements of the spindle. Other macromolecules including RNA and lipids also associate with spindles, but their spindle function, if any, is unknown. Poly(ADP-ribose) (PAR) is a large, branched, negatively charged polymeric macromolecule whose polymerization onto acceptor proteins is catalysed by a family of poly(ADP-ribose) polymerases (PARPs). Several PARPs localize to the spindle in vertebrate cells, suggesting that PARPs and/or PAR have a role in spindle function. Here we show that PAR is enriched in the spindle and is required for spindle function--PAR hydrolysis or perturbation leads to rapid disruption of spindle structure, and hydrolysis during spindle assembly blocks the formation of bipolar spindles. PAR exhibits localization dynamics that differ from known spindle proteins and are consistent with a low rate of turnover in the spindle. Thus, PAR is a non-proteinaceous, non-chromosomal component of the spindle required for bipolar spindle assembly and function.     

Crystal structure of spinach major light-harvesting complex at 2.72 A resolution

The major light-harvesting complex of photosystem II (LHC-II) serves as the principal solar energy collector in the photosynthesis of green plants and presumably also functions in photoprotection under high-light conditions. Here we report the first X-ray structure of LHC-II in icosahedral proteoliposome assembly at atomic detail. One asymmetric unit of a large R32 unit cell contains ten LHC-II monomers. The 14 chlorophylls (Chl) in each monomer can be unambiguously distinguished as eight Chla and six Chlb molecules. Assignment of the orientation of the transition dipole moment of each chlorophyll has been achieved. All Chlb are located around the interface between adjacent monomers, and together with Chla they are the basis for efficient light harvesting. Four carotenoid-binding sites per monomer have been observed. The xanthophyll-cycle carotenoid at the monomer-monomer interface may be involved in the non-radiative dissipation of excessive energy, one of the photoprotective strategies that have evolved in plants.