背靠背换流站换相失败仿真分析

开展背靠背系统换相失败的研究,对防止换相失败的发生及减小换相失败对系统运行的影响具有十分重要的意义.介绍了换相失败及引起换相失败的原因,分析了换相失败的过程.在PSCAD/EMTDC中对灵宝换流站换相失败进行了仿真,分析了换相失败后直流电压、直流电流、直流功率、逆变侧交流母线电压、整流侧触发角、逆变侧关断角的变化情况.仿真结果可以为制定避免换相失败或控制换相失败发展的措施提供参考.     

Summer habitat use and feeding of juvenile Arctic charr,Salvelinus alpinus,in the Canadian High Arctic

Abstract – Owing to limited knowledge of the habitat use and diet of juvenile Arctic charr from the High Arctic, particularly young‐of‐the‐year (YOY), we assembled data obtained from samples taken in and around Lake Hazen, Nunavut, Canada, to assess juvenile habitat use and feeding. Juvenile charr demonstrated a preference for stream environments, particularly those fed by warm upstream ponds. Charr occupying both stream and nearshore lake habitats were found to feed similarly, with chironomids occurring most frequently in diets. Some older stream‐dwelling charr preyed on smaller, younger Arctic charr. Preferred stream occupancy is likely mediated by physical barriers created mainly by water velocity, and by distance from the lake, lake‐ice dynamics, low water depth, and turbidity. Water velocities resulted in stream habitat segregation by size, with YOY mainly found in low‐velocity pools and back eddies adjacent to stream banks, but not in water velocities >0.1 m·s^?1. Greatest charr densities in streams were found in small, shallow, slow‐flowing side channels, which are highly susceptible to drought. Under predicted climate change scenarios, streams fed by small ponds will be susceptible to intermittent flow conditions, which could result in increased competition among juvenile charr for the remaining stream habitats. In addition, glacier‐fed streams are likely to experience increased flow conditions that will exacerbate physical barriers created by water velocity and further reduce the availability of preferred stream habitat.     

Immunobiological role of llama heavy-chain antibodies against a bacterial beta-lactamase

In 1993, a fraction of antibodies (Abs) devoid of L chain was found naturally occurring in the Camelidae. They were found to lack L chains, as well as the first constant heavy-chain domain (CH(1)) and therefore they were named "heavy-chain Abs" (HCAbs). Subsequent studies focused on the functional, structural and biochemical properties of recombinant variable fragments (rVHHs) of HCAbs. It was stated that rVHHs have an augmented capacity to interact with "partially hidden" epitopes, like enzymes active sites, and have an increased stability to thermal and chemical aggression. It has been suggested that these unconventional Abs could represent an evolutionary advantage, being more efficient than conventional Abs to inhibit microbial enzymes, and thus exerting a more protective immune response against pathogens. The present work focuses on the immunobiological role of HCAbs, in their capacity to inhibit microbial enzymes. Two animal models were selected, comprising a model for common vertebrates without HCAbs (rabbits), and a model for vertebrates with both conventional and unconventional Abs (Lama glama). A recombinant bacterial beta-lactamase (CTX-M-2) was selected as the microbial enzymatic antigen. After conventional immunization schedules, neither serum titers nor serum inhibitory capacity showed significant differences when rabbits and llamas were compared. These results indicate that the a priori assumption that the adaptive immune system of camelids could be better "prepared" to respond to bacterial enzymes because of the presence of HCAbs, is not always accurate. Furthermore, when the different llama antibody isotypes and subclasses were purified, it was demonstrated that the inhibitory capacity of total serum was due exclusively to IgG(1). HCAbs not only failed to inhibit CTX-M-2, but instead they activated its enzymatic activity. Altogether, these results indicate that the hypotheses extrapolated from the rVHHs properties need to be revised; the real role of HCAbs in vivo remains unknown, as well as their evolutionary cause.