• Journal of the Institute of Electronics and Information Engineers
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• v.52 no.9
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• pp.63-73
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• 2015

This work proposes a 2-channel time-interleaved (T-I) 10b 120MS/s pipeline SAR ADC minimizing offset mismatch between channels without any calibration scheme. The proposed ADC employs a 2-channel SAR and T-I topology based on a 2-step pipeline ADC with 4b and 7b in the first and second stage for high conversion rate and low power consumption. Analog circuits such as comparator and residue amplifier are shared between channels to minimize power consumption, chip area, and offset mismatch which limits the ADC linearity in the conventional T-I architecture, without any calibration scheme. The TSPC D flip-flop with a short propagation delay and a small number of transistors is used in the SAR logic instead of the conventional static D flip-flop to achieve high-speed SAR operation as well as low power consumption and chip area. Three separate reference voltage drivers for 4b SAR, 7b SAR circuits and a single residue amplifier prevent undesirable disturbance among the reference voltages due to each different switching operation and minimize gain mismatch between channels. High-frequency clocks with a controllable duty cycle are generated on chip to eliminate the need of external complicated high-frequency clocks for SAR operation. The prototype ADC in a 45nm CMOS technology demonstrates a measured DNL and INL within 0.69LSB and 0.77LSB, with a maximum SNDR and SFDR of 50.9dB and 59.7dB at 120MS/s, respectively. The proposed ADC occupies an active die area of 0.36mm2 and consumes 8.8mW at a 1.1V supply voltage.

• Journal of the Korean Magnetic Resonance Society
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• v.12 no.1
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• pp.1-13
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• 2008

Acetyl-CoA carboxylase (ACC) catalyzes the first step in fatty acid biosynthesis: the synthesis of malonyl-CoA from acetyl-CoA. As essential regulators of fatty acid biosynthesis and metabolism, ACCs are regarded as therapeutic targets for the treatment of metabolic diseases such as obesity, In ACC, the biotinoyl domain performs a critical function by transferring an activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, followed by carboxyl transfer to malonyl-CoA. Despite the intensive research on this enzyme, only the bacterial and yeast ACC structures are currently available, To explore the mechanism of ACC holoenzyme function, we determined the structure of the biotinoyl domain of human ACC2 and analyze its characteristics using NMR spectroscopy. The 3D structure of the hACC2 biotinoyl domain has a similar folding topology to the previously determined domains from E. coli and P. Shermanii, however, the 'thumb' structure is absent in the hACC2 biotinoyl domain. Observations of the NMR signals upon the biotinylation indicate that the biotin group of hACC2 does not affect the structure of the biotinoyl domain, while the biotin group for E. coli ACC interacts directly with the thumb residues that are not present in the hACC2 structure. These results imply that, in the E. coli ACC reaction, the biotin moiety carrying the carboxyl group from BC to CT can pause at the thumb of the BCCP domain. The human biotinoyl domain, however, lacks the thumb structure and does not have additional non-covalent interactions with the biotin moiety; thus, the flexible motion of the biotinylated lysine residue must underlie the "swinging arm" motion. This study provides insight into the mechanism of ACC holoenzyme function and supports the "swinging arm" model in human ACCs.