Discrete fast Fourier transform （FFT） has been widely applied to signal spectral analysis and can figure out the entire bandwidth spectrum of a signal. However, the fine structure of high resolution spectrum in a na...Discrete fast Fourier transform （FFT） has been widely applied to signal spectral analysis and can figure out the entire bandwidth spectrum of a signal. However, the fine structure of high resolution spectrum in a narrow bandwidth is required in some applications. If regular FFT is still used to figure out the high resolution spectrum, it will result in addition of data and at last sharply increase of computation and storage. Therefore, FFT is inefficient and a new method must be put forward. In the paper, the principle of zoom FFT technique based on complex modulation, its application to development of SLF/ELF receiver and how to obtain high resolution spectrum using the new technique are introduced in detail and also the theoretical and test results are presented.展开更多
In order to reveal the phenomenon of R. rugose pollination incompatibility, the full-length cDNA sequence of S Locus F-box Gene was cloned for the first time from the pollen of Rosa rugose “Zilong wochi” with RT-PCR...In order to reveal the phenomenon of R. rugose pollination incompatibility, the full-length cDNA sequence of S Locus F-box Gene was cloned for the first time from the pollen of Rosa rugose “Zilong wochi” with RT-PCR and RACE methods and named as RrSLF. The full-length cDNA is 1236 bp with an open reading frame of 1122 bp, encoding 343 amino acids. The derived protein has a molecular weight of 43.7 kD, a calculated pI of 6.24, an F-box conserved domain at position 343 - 741, and belongs to F-box family. The derived protein is a Hydrophobicity protein secreted into the cytoplasm. There is no transmembrane domain and no signal peptide cleavage site, twenty-one Ser phosphorylation sites, seven Thr phosphorylation sites, seven Tyr phosphorylation sites, two N-glycosylation sites, and no O-glycosylation sites. There are 22.25% α-helixes, 31.37% random coil, 32.17% extended peptide chain, and 14.21% β-corner structure. This protein and the SFB/SLF protein from Rosaceae Prunus fruit, including Prunus speciose, share a sequence homology of 59% - 61%;all of the proteins contain an F-box conserved domain, two hypervariable regions HVa, HVb, and two variable regions V1, V2. Furthermore, their phylogenetic relationships are consistent with their traditional classifications. These results were meaningful to reveal the molecular mechanism of Rosa rugose pollination incompatibility and improve the theory and techniques of breeding ornamental Rosa rugose.展开更多
基金"The Study of ELF Receiver" from Ministry of Science and Technology (2001BA601B03-01-03).
文摘Discrete fast Fourier transform （FFT） has been widely applied to signal spectral analysis and can figure out the entire bandwidth spectrum of a signal. However, the fine structure of high resolution spectrum in a narrow bandwidth is required in some applications. If regular FFT is still used to figure out the high resolution spectrum, it will result in addition of data and at last sharply increase of computation and storage. Therefore, FFT is inefficient and a new method must be put forward. In the paper, the principle of zoom FFT technique based on complex modulation, its application to development of SLF/ELF receiver and how to obtain high resolution spectrum using the new technique are introduced in detail and also the theoretical and test results are presented.
文摘In order to reveal the phenomenon of R. rugose pollination incompatibility, the full-length cDNA sequence of S Locus F-box Gene was cloned for the first time from the pollen of Rosa rugose “Zilong wochi” with RT-PCR and RACE methods and named as RrSLF. The full-length cDNA is 1236 bp with an open reading frame of 1122 bp, encoding 343 amino acids. The derived protein has a molecular weight of 43.7 kD, a calculated pI of 6.24, an F-box conserved domain at position 343 - 741, and belongs to F-box family. The derived protein is a Hydrophobicity protein secreted into the cytoplasm. There is no transmembrane domain and no signal peptide cleavage site, twenty-one Ser phosphorylation sites, seven Thr phosphorylation sites, seven Tyr phosphorylation sites, two N-glycosylation sites, and no O-glycosylation sites. There are 22.25% α-helixes, 31.37% random coil, 32.17% extended peptide chain, and 14.21% β-corner structure. This protein and the SFB/SLF protein from Rosaceae Prunus fruit, including Prunus speciose, share a sequence homology of 59% - 61%;all of the proteins contain an F-box conserved domain, two hypervariable regions HVa, HVb, and two variable regions V1, V2. Furthermore, their phylogenetic relationships are consistent with their traditional classifications. These results were meaningful to reveal the molecular mechanism of Rosa rugose pollination incompatibility and improve the theory and techniques of breeding ornamental Rosa rugose.
