A5082090301- Enzyme Structure and Function
- Heat shock proteins research
- Protein Structure and Dynamics
- Advanced Electron Microscopy Techniques and Applications
- Conflict of Laws and Jurisdiction
- Metal-Catalyzed Oxygenation Mechanisms
- Metalloenzymes and iron-sulfur proteins
- Toxin Mechanisms and Immunotoxins
- Analog and Mixed-Signal Circuit Design
- Advanced NMR Techniques and Applications
- Weed Control and Herbicide Applications
- Machine Learning in Materials Science
- Physics of Superconductivity and Magnetism
- Seed Germination and Physiology
- Neurobiology and Insect Physiology Research
- Advanced MEMS and NEMS Technologies
- Global Financial Regulation and Crises
- International Arbitration and Investment Law
- Low-power high-performance VLSI design
- Insect symbiosis and bacterial influences
- Plant tissue culture and regeneration
- Endoplasmic Reticulum Stress and Disease
- Innovative Energy Harvesting Technologies
- Radio Frequency Integrated Circuit Design
- Dispute Resolution and Class Actions
Seoul National University
2021-2025
Sunchon National University
2023
University of Michigan
2010-2013
An 8.75 mm <sup xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink">3</sup> sensor system is implemented with a near-threshold ARM Cortex-M3 core, custom 3.3 fW leakage-per-bit SRAM, two 1 xmlns:xlink="http://www.w3.org/1999/xlink">2</sup> solar cells, thin-film Li-ion battery, and an integrated power management unit. The 2.1 ¿W enters 100 pW data-retentive sleep state between measurements harvests energy from the cells to enable nearly perpetual operation.
An 8.75 mm <sup xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink">3</sup> microsystem targeting temperature sensing achieves zero-net-energy operation using energy harvesting and ultra-low-power circuit techniques. A 200 nW sensor measures with -1.6 xmlns:xlink="http://www.w3.org/1999/xlink">°</sup> C/+3 C accuracy at a rate of 10 samples/sec. 28 pJ/cycle, 0.4 V, 72 kHz ARM Cortex-M3 microcontroller processes data 3.3 fW leakage per bit SRAM. Two 1...
Abstract Proper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) phosducin-like proteins (PhLPs) to facilitate folding eukaryotic proteins. Using cryoEM biochemical analyses, we determine the ATP-driven cycle TRiC-PFD-PhLP2A interaction. PhLP2A binds open apo-TRiC through polyvalent domain-specific contacts its chamber’s equatorial apical regions. N-terminal...
While it is now accepted that the microbiome has strong impacts on animal growth promotion, exact mechanism remained elusive. Here we show microbiome-emitted scents contain volatile somatotrophic factors (VSFs), which promote host in an olfaction-independent manner Drosophila. We found inhaled VSFs are readily sensed by olfactory receptor 42b non-neuronally expressed subsets of tracheal airway cells, enteroendocrine and enterocytes. Olfaction-independent sensing activates airway-gut-brain...
Transmission electron microscopy (TEM) is a crucial analysis method in materials science and structural biology, as it offers high spatiotemporal resolution for characterization reveals structure-property relationships dynamics at atomic molecular levels. Despite technical advancements EM, the nature of beam makes EM imaging inherently detrimental to even low-dose applications. We introduce SHINE, Self-supervised High-throughput Image denoising Neural network Electron microscopy,...
Accurate folding of proteins in living cells often requires the cooperative support molecular chaperones. Eukaryotic group II chaperonin TRiC accomplishes this task by providing a chamber for substrate that is regulated an ATP hydrolysis-dependent cycle. Once delivered to and recognized TRiC, nascent enters undergoes release stepwise manner. During process, subunits cochaperones such as prefoldin (PFD) phosducin-like (PhLPs) interact with assist overall process substrate-specific Coevolution...
Abstract Formate dehydrogenase (FDH) is critical for the conversion between formate and carbon dioxide. Despite its importance, structural complexity of FDH difficulties in production enzyme have made elucidating unique physicochemical properties challenging. Here, we purified recombinant Methylobacterium extorquens AM1 (MeFDH1) used cryo-electron microscopy to determine structure. We resolved a heterodimeric MeFDH1 structure at resolution 2.8 Å, showing noncanonical active site...
A logic-compatible 2T dual-Vt embedded DRAM (eDRAM) is proposed for ultra-small sensing systems to achieve 8× longer retention time, 5× lower refresh power and 30% reduced area compared with the lowest eDRAM previously reported. With an area-efficient single inverter scheme designed R/W speed compatibility ultra-low processors, 58% array efficiency maintained memories as small 2kb few 32 bits per bitline.
Abstract Proper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) phosducin-like proteins (PhLPs) to facilitate the folding eukaryotic proteins. Using cryoEM biochemical analyses, we determine ATP-driven cycle TRiC-PFD-PhLP2A interaction. In open TRiC state, PhLP2A binds chamber’s equator while its N-terminal H3-domain apical domains CCT3/4, thereby displacing PFD...
Cryopreservation, storing biological material in liquid nitrogen (LN, -196 °C), offers a valuable option for the long-term conservation of non-orthodox seeds and vegetatively propagated species sector agrobiodiversity wild flora. Although large-scale cryobanking germplasm collections has been increasing worldwide, wide application cryopreservation protocol is hampered by lack universal protocols, among others. This study established systematic approach to developing droplet-vitrification...
SUMMARY The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of β-tubulin using human Prefoldin and TRiC. We find unstructured delivered by to open chamber followed closure. CryoEM resolves four near-atomic resolution structures containing progressively folded intermediates within closed chamber, culminating in native tubulin. This substrate pathway...
Abstract Cryogenic‐electron microscopy (cryo‐EM) is the preferred method to determine 3D structures of proteins and study diverse material systems that intrinsically have radiation or air sensitivity. Current cryo‐EM sample preparation methods provide limited control over quality, which limits efficiency high throughput structure analysis. This partly because it difficult thickness vitreous ice embeds specimens, in range nanoscale, depending on size type materials interest. Thus, there a...
Cryo-electron microscopy (cryo-EM) is a revolutionary technique to study the three-dimensional structure of macromolecules and theirs complexes at molecular resolution. The first step in preparing samples for cryo-EM select optimize right grid specimen. This screening process needs consideration many aspects including concentration stability specimen, compatibility with material optimum ice thickness across grid. Importantly, best signal-to-noise ratio (SNR) micrograph closely related...