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RISS 인기검색어
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- 저자 : ( Ruiyang Xu ) (검색결과 2 건)
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Modified WFRFT-based Transform Domain Communication System Incorporating with Spectrum Mismatching
( Ruiyang Xu ),( Xinyu Da ),( Yuan Liang ),( Hang Hu ) 한국인터넷정보학회 2018 KSII Transactions on Internet and Information Syst Vol.12 No.10
The transform domain communication system (Hereinafter referred to as TDCS) takes on numerous advantages, inclusive of anti-jamming and low probability of detection. Yet its application is confined by the consistent spectrum in the transmitter and receiver, which is not possible in the case of a huge distance exsits between them. In this paper, a TDCS based modified weighted fractional fourier transform (WFRFT) is proposed to solve the problem resulting from spectrum mismatching for TDCS application. The amplitude and phase information are incorporated with the TDCS signals and transmit to the receiver together in the wake of a modified WFRFT. The basic function and the TDCS signals shall be accessible to the receivers in the wake of an inverse WFRFT transform, which make sure that the original information can be demodulated properly. The system’s reliability while transmitting signals with different modulation methods and with spectrum mismatching is demonstrated by bit error rate (BER). In the meantime, the constellations of the signals and the BER performances at the eavesdropper demonstrate the proposed system is better secured.
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Rui Yang,Yuqian Liu,Jingjing Xu,Wenting Shang,Xiaoyuan Zhang,Yongjin Wang,Chris Blanchard,Zhongkai Zhou 한국식품과학회 2018 Food Science and Biotechnology Vol.27 No.6
Epigallocatechin gallate (EGCG) is sensitive to heat thus its application in food industry is limited. In this work, rice bran albumin protein (RAP) was used as a carrier for EGCG. RAP-EGCG complexes (RAPE) were prepared with the binding number n of 0.0505:1 (EGCG: RAP, w/w) and binding constant K of (0.74 ± 0.002) 9 104 M-1, which suggests that hydrogen bond/van der Waals forces played important roles in such binding. FTIR analysis demonstrated that EGCG could induce the secondary structure changes of RAP above the ratio of 1.92:1 (EGCG:RAP, w/w). Dynamic light scattering and scanning electron microscope results showed that EGCG could trigger RAP association. Furthermore, the EGCG stability in RAPE was significantly improved than that of free EGCG in 10–60 C. The antioxidant ability of EGCG in RAPE was partially retained. These findings prove that RAP is a potential carrier for polyphenols and is beneficial for mechanism investigation between protein and polyphenols.
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