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Green Cooperative Sensing Scheme in Heterogeneous Networks
( Lifei Shen ),( Jian Liu ),( Xinxin Tan ),( Lei Wang ) 한국인터넷정보학회 2018 KSII Transactions on Internet and Information Syst Vol.12 No.2
Cognitive radio technology is still the key technology of future mobile communication systems. Previous studies have focused on improving spectrum utilization and less energy consumption. In this paper, we propose an Overhead Reduced Scheme (ORS) for green cooperative spectrum sensing. Compared to traditional cooperative sensing scheme, ORS scheme divides the sensing time into three time slots and selects the best multi-mode user to report decisions. In consideration of reporting channel deviation, we derive closed-form expressions for detection probability and false alarm probability of ORS scheme based on Rayleigh fading channel. Simulation results show that ORS scheme can improve the perception accuracy while reducing the perceived delay and energy consumption in the process of perception, so as to realize the green communication.
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Yi Luo,Lifei Sun,Zhen Zhu,Wei Ran,Qirong Shen 한국미생물학회 2013 The journal of microbiology Vol.51 No.3
A newly discovered alkaline antifungal protease named P6 from Bacillus subtilis N7 was purified and partially characterized. B. subtilis N7 culture filtrates were purified by 30–60% (NH4)2SO4 precipitation, anion-exchange chromatography and gel filtration chromatography. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) revealed a single band of 41.38 kDa. Peptide sequence of protease P6 was determined using a 4800 Plus MALDI TOF/TOFTM Analyzer System. Self-Formed Adaptor PCR (SEFA-PCR) was used to amplify the 1,149 bp open read frame of P6. Dimensional structure prediction using Automatic Modeling Mode software showed that the protease P6 consisted of two β-barrel domains. Purified P6 strongly inhibited spore and mycelium growth of Fusarium oxysporum f. sp. cucumerium (FOC) by causing hypha lysis when the concentration was 25 μg/ml. Characterization of the purified protease indicated that it had substrate specificity for gelatin and was highly active at pH 8.0–10.6 and 70°C. The P6 protease was inhibited by EDTA (2 mmol/L), phenyl methyl sulfonyl fluoride (PMSF, 1 mmol/L), Na+, Fe3+, Cu2+, Mg2+ (5 mmol/L each) and H2O2 (2%, v/v). However, protease activity was activated by Ca2+, K+, Mn2+ (5 mmol/L each), mercaptoethanol (2%, v/v) and Tween 80 (1%, v/v). In additon, activity was also affected by organic solvents such as acetone, normal butanol and ethanol, but not hexane (25%, v/v each).
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