HIRFL新B1聚束器冷却系统设计

在利用 MAFIA程序计算得到的新 B1聚束器腔体表面电流分布的基础上 ,提出了新 B1聚束器的冷却方案 ,并计算了水流及水管表面的电流分布 ,得到了冷却所需要的流量。最后估计了由于工作温度的升高所引起的并联阻抗的减小及频率的漂移。

HIRFL新B1聚束器耦合环的设计与计算

通过将聚束器腔体等效为 RLC并联回路 ,求得了功率馈入耦合环与腔体的互感及自感的公式 ,根据对腔体的计算结果求出了在聚束器的工作频段内达到阻抗匹配所要求的互感变化范围 ,并在该互感变化范围内设计了可移动的耦合电感环 ,计算了它的自感及整个腔体的剩余电感。

三维电磁场数值模拟在腔体设计中的应用——新B1聚束器的腔体设计

为了提高HIRFL的束流指标，特别是束流强度，以满足放射性次级束流线（RIBLL）及大科学工程兰州重离子冷却储存环（CSR）对束流的更高要求，目前 HIRFL 正在进行很多方面的改造，其中之一便是建造一台新聚束器B1来改善注入器 SFC 与主加速器SSC之间的给向匹配。为了克服非线性效应，新B1设计工作在多模式下，频率范围为 22MHz～54MHz，最高电压达110kV。由于较宽的工作频率范围、较高的电压及有限的空间位置，新B1聚束器的腔体设计存在许多困难。本论文的主要工作便是设计新B1聚束器的腔体。主要工作可分为三部分：1．腔体设计：在这部分，我们利用三维电磁场模拟程序－MAFIA，辅之以传输线近似法，设计出了满足物理要求的腔体方案，给出了模拟计算所得到了的腔体主要参数，并就这些参数的可信度进行了评估。2．耦合环设计：在这部分，我们利用 MAFIA 模拟得到的结果，从腔体的等效集总电路出发，推导出了耦合环参数与腔体特性参数之间的关系，并设计出了满足物理要求的耦合方案。3．冷却系统设计：这部分的主要工作为从对流、传导换热理论出发，结合新B1的实际，建立了自己的传热模型，设计了新B1腔体的冷却系统，计算了腔体的最高工作温度，并讨论了工作温度的升高对腔体性能的影响。另外，在论文的最后一章还介绍了其它一些工作，主要包括SFC中 Dee 电压分布计算、原B2腔体的实验研究以及原B1腔体的传输线近似法模拟。

Otimização do método de Elisa indireto não competitivo para detecção e quantificação de aflatoxina B1 em cereais.

2007

Chemistry of B1- and B10- boranes containing halogen or pseudohalogen groups

The research described in this thesis involved the chemistry of borane-species which contain one or more halide or pseudohalide groups. Both monoboron species e.g. [BH3X]- and "cluster" borane species e.g. [B10H9X]2- and I-Se B11H10 were studied. The first chapter is a review of the syntheses, properties and reactions of halide and pseudohalide species containing from one to ten boron atoms. Chapter Two is a theoretical investigation of' the electronic and molecular structures of two series of boranes i. e. [BH3X]- and [B10H9X]2- where X = H, CI, CN, NCS, SCN and N3. The calculational method used was the Modified Neglect of Differential Overlap (MNDO) method of Dewar et al. The results were compared where possible with experimental results such as the X-ray crystallographically determined structures of [BH3CI]- and [B10H10]2-. Chapter Three concerns halogenated selenaborane clusters and reports an improved synthesis of 12-Br-SeB11H10 and the first structural data for a simple non-metal containing selenaborane cage with the X-ray crystallographically determined structure of 12-1-SeB11H10. Finally, an indepth n.m.r. study of Se2B9H9 is also reported together with attempts to halogenate this compound. The last two chapters are based on single boron systems. Chapter Four concerns the synthetic routes to amine-boranes and -cyanoboranes from [BH4]- and [BH3CN]- substrates. This chapter discusses some difficulties encountered when polyamines were used in these reactions. The characterisation of an unusual ketone isolated from some of these reactions, the X-ray crystallographically determined structure of 4-dimethylamino-pyridine-cyanoborane and a new route to pyrazabole dimeric species are also discussed. The final chapter reports on work carried out at producing BH2X (X = H, CN) adducts of aminophosphines. Three routes were attempted to generate P-B and N-B bonded species with varying degrees of success. Some unusual products of these reactions are discussed including [Ph2(O) PPPh2 ] [Ph2NH]2, the structure of which was determined by X-ray crystallography.

Nuclear import of Cdk/cyclin complexes: identification of distinct mechanisms for import of Cdk2/cyclin E and Cdc2/cyclin B1.

Reversible phosphorylation of nuclear proteins is required for both DNA replication and entry into mitosis. Consequently, most cyclin-dependent kinase (Cdk)/cyclin complexes are localized to the nucleus when active. Although our understanding of nuclear transport processes has been greatly enhanced by the recent identification of nuclear targeting sequences and soluble nuclear import factors with which they interact, the mechanisms used to target Cdk/cyclin complexes to the nucleus remain obscure; this is in part because these proteins lack obvious nuclear localization sequences. To elucidate the molecular mechanisms responsible for Cdk/cyclin transport, we examined nuclear import of fluorescent Cdk2/cyclin E and Cdc2/cyclin B1 complexes in digitonin-permeabilized mammalian cells and also examined potential physical interactions between these Cdks, cyclins, and soluble import factors. We found that the nuclear import machinery recognizes these Cdk/cyclin complexes through direct interactions with the cyclin component. Surprisingly, cyclins E and B1 are imported into nuclei via distinct mechanisms. Cyclin E behaves like a classical basic nuclear localization sequence-containing protein, binding to the alpha adaptor subunit of the importin-alpha/beta heterodimer. In contrast, cyclin B1 is imported via a direct interaction with a site in the NH2 terminus of importin-beta that is distinct from that used to bind importin-alpha.

Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1.

Activation of the Cyclin B/Cdc2 kinase complex triggers entry into mitosis in all eukaryotic cells. Cyclin B1 localization changes dramatically during the cell cycle, precipitously transiting from the cytoplasm to the nucleus at the beginning of mitosis. Presumably, this relocalization promotes the phosphorylation of nuclear targets critical for chromatin condensation and nuclear envelope breakdown. We show here that the previously characterized cytoplasmic retention sequence of Cyclin B1, responsible for its interphase cytoplasmic localization, is actually an autonomous nuclear export sequence, capable of directing nuclear export of a heterologous protein, and able to bind specifically to the recently identified export mediator, CRM1. We propose that the observed cytoplasmic localization of Cyclin B1 during interphase reflects the equilibrium between ongoing nuclear import and rapid CRM1-mediated export. In support of this hypothesis, we found that treatment of cells with leptomycin B, which disrupted Cyclin B1-CRM1 interactions, led to a marked nuclear accumulation of Cyclin B1. In mitosis, Cyclin B1 undergoes phosphorylation at several sites, a subset of which have been proposed to play a role in Cyclin B1 accumulation in the nucleus. Both CRM1 binding and the ability to direct nuclear export were affected by mutation of these phosphorylation sites; thus, we propose that Cyclin B1 phosphorylation at the G2/M transition prevents its interaction with CRM1, thereby reducing nuclear export and facilitating nuclear accumulation.

The liver kinase B1 is a central regulator of T cell development, activation, and metabolism.

T cell activation leads to engagement of cellular metabolic pathways necessary to support cell proliferation and function. However, our understanding of the signal transduction pathways that regulate metabolism and their impact on T cell function remains limited. The liver kinase B1 (LKB1) is a serine/threonine kinase that links cellular metabolism with cell growth and proliferation. In this study, we demonstrate that LKB1 is a critical regulator of T cell development, viability, activation, and metabolism. T cell-specific ablation of the gene that encodes LKB1 resulted in blocked thymocyte development and a reduction in peripheral T cells. LKB1-deficient T cells exhibited defects in cell proliferation and viability and altered glycolytic and lipid metabolism. Interestingly, loss of LKB1 promoted increased T cell activation and inflammatory cytokine production by both CD4(+) and CD8(+) T cells. Activation of the AMP-activated protein kinase (AMPK) was decreased in LKB1-deficient T cells. AMPK was found to mediate a subset of LKB1 functions in T lymphocytes, as mice lacking the α1 subunit of AMPK displayed similar defects in T cell activation, metabolism, and inflammatory cytokine production, but normal T cell development and peripheral T cell homeostasis. LKB1- and AMPKα1-deficient T cells each displayed elevated mammalian target of rapamycin complex 1 signaling and IFN-γ production that could be reversed by rapamycin treatment. Our data highlight a central role for LKB1 in T cell activation, viability, and metabolism and suggest that LKB1-AMPK signaling negatively regulates T cell effector function through regulation of mammalian target of rapamycin activity.