High-Speed Frequency Modulation of a 460-GHz Gyrotron for Enhancement of 700-MHz DNP-NMR Spectroscopy

Idehara, T., et al., High-Speed Frequency Modulation of a 460-GHz Gyrotron for Enhancement of 700-MHz DNP-NMR Spectroscopy. J Infrared Milli Terahz Waves, 2015: p. 1-11.


The high-speed frequency modulation of a 460-GHz Gyrotron FU CW GVI (the official name in Osaka University is Gyrotron FU CW GOI) was achieved by modulation of acceleration voltage of beam electrons. The modulation speed fm can be increased up to 10 kHz without decreasing the modulation amplitude δf of frequency. The amplitude δf was increased almost linearly with the modulation amplitude of acceleration voltage ΔVa. At the ΔVa=1 kV, frequency spectrum width df was 50 MHz in the case of fm<10 kHz. The frequency modulation was observed as both the variation of the IF frequency in the heterodyne detection system measured by a high-speed oscilloscope and the widths of frequency spectra df measured on a frequency spectrum analyzer. Both results well agree reasonably. When fm exceeds 10 kHz, the amplitude δf is decreased gradually with increasing fm because of the degradation of the used amplifier in response for high-speed modulation. The experiment was performed successfully for both a sinusoidal wave and triangle wave modulations. We can use the high-speed frequency modulation for increasing the enhancement factor of the dynamic nuclear polarization (DNP)-enhanced nuclear magnetic resonance (NMR) spectroscopy, which is one of effective and attractive methods for the high-frequency DNP-NMR spectroscopy, for example, at 700 MHz. Because the sensitivity of NMR is inversely proportional to the frequency, high-speed frequency modulation can compensate the decreasing the enhancement factor in the high-frequency DNP-NMR spectroscopy and keep the factor at high value. In addition, the high-speed frequency modulation is useful for frequency stabilization by a PID control of an acceleration voltage by feeding back of the fluctuation of frequency. The frequency stabilization in long time is also useful for application of a DNP-NMR spectroscopy to the analysis of complicated protein molecules.

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