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Showing 1–10 of 10 results
Advanced filters: Author: Duyoung Min Clear advanced filters

  • Conventional protein oxidation pathways typically involve free diffusion of reactive oxygen species (ROS), which primarily attack the protein surface. Here, the authors report a pathway of protein damage, O2-confined photooxidation, where O2 is captured in protein cavities and subsequently converted into multiple ROS which attack the protein interior.

    • Seoyoon Kim
    • Eojin Kim
    • Duyoung Min
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-19

  • Oxidative damage to intracellular membrane proteins is critical to cells. Here, the authors use a water-oxidizing photocatalyst, generating ∙OH even under hypoxia, to show that membrane-specific protein oxidation triggers pyroptosis via non-canonical inflammasomes.

    • Chaiheon Lee
    • Mingyu Park
    • Tae-Hyuk Kwon
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Water plays an essential role in enzyme catalysis, but direct observations linking enzyme catalysis and active-site water pose a significant challenge due to experimental difficulties. Here, the authors employ an ultraviolet photolysis technique with temperature-controlled X-ray crystallography to track the catalytic pathway of carbonic anhydrase II at 1.2 Å resolution.

    • Jin Kyun Kim
    • Seon Woo Lim
    • Chae Un Kim
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • Single-molecule experiments reveal the unfolding and refolding landscape of the rhomboid protease GlpG in a native-like lipid membrane. GlpG unravels cooperatively in a single step and has a large unfolding barrier, making for a long-lived folded state.

    • Duyoung Min
    • Robert E Jefferson
    • Tae-Young Yoon
    Research
    Nature Chemical Biology
    Volume: 11, P: 981-987

  • Interactions between (SNARE) proteins on vesicle and target membranes provide the force necessary to drive membrane fusion. By applying piconewton forces to single SNARE complexes, the authors identify a partially assembled intermediate state that reveals how force is generated in a consistent direction.

    • Duyoung Min
    • Kipom Kim
    • Tae-Young Yoon
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-10

  • The typical method for DNA origami fabrication uses thermal annealing of staples to a longer DNA scaffold. Here, the authors present a mechanical method to control the folding pathway, which instead relies on stretching the DNA scaffold in magnetic tweezers, prior to staple incorporation.

    • Wooli Bae
    • Kipom Kim
    • Tae-Young Yoon
    Research
    Nature Communications
    Volume: 5, P: 1-8

  • A single-molecule forced unfolding of E. coli chloride transporter ClC-ec1 shows that the N- and C-terminal halves of the protein unfold independently, with exposed polar surfaces stabilized by membrane lipid head groups and water.

    • Duyoung Min
    • Robert E. Jefferson
    • James U. Bowie
    Research
    Nature Chemical Biology
    Volume: 14, P: 489-496