{"id":2935,"date":"2025-08-15T14:24:53","date_gmt":"2025-08-15T05:24:53","guid":{"rendered":"https:\/\/pf-form.kek.jp\/sbrc\/?p=2935"},"modified":"2025-08-19T08:40:57","modified_gmt":"2025-08-18T23:40:57","slug":"seminar3","status":"publish","type":"post","link":"https:\/\/pf-form.kek.jp\/sbrc\/seminar3\/","title":{"rendered":"SBRC Seminar"},"content":{"rendered":"\n

<\/p>\n\n\n\n

\u201cStructural Studies of Biomolecular and Supramolecular Complexes<\/strong>\u201d<\/h2>\n\n\n\n

_<\/p>\n\n\n\n

Date and Time<\/h2>\n\n\n\n

4:00 PM – Friday, August 22, 2025<\/p>\n\n\n\n

Location<\/h2>\n\n\n\n

KEK CryoEM building<\/p>\n\n\n\n

<\/p>\n\n\n

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Speakers: Ilkin Yapici<\/h2>\n\n\n\n
\"\"<\/figure>\n\n\n\n

Koc University<\/p>\n\n\n\n

Abstract<\/h2>\n\n\n\n

High-resolution structural studies continue to drive progress in both antibiotic development and neurodegenerative disease research. Building on our previous work using serial femtosecond X-ray crystallography (SFX) at XFELs to resolve 30S and 50S ribosomal subunits at ambient temperature, we are now extending our structural investigations to intact 70S ribosomes using single-particle cryo-electron microscopy. These cryo-EM studies aim to elucidate how next-generation antibiotics interact with the bacterial translation machinery, offering new insights into drug binding, resistance mechanisms, and ribosome functional dynamics under near-native conditions.<\/p>\n\n\n\n

In parallel, we are investigating the structural features of ALS-linked superoxide dismutase 1 (SOD1) aggregates, with a focus on the H71Y mutant identified in Turkish patients. Cryo-EM and cryo-electron tomography (cryo-ET) reveal that this variant forms long, unbranched amyloid-like fibers with a characteristic hollow-core morphology and accelerated aggregation kinetics. Guided by these structural insights, we are screening a panel of hybrid small molecules incorporating radical-scavenging, metal-chelating, and ferroptosis-inhibiting elements. Preliminary data suggest these compounds may interfere with fiber growth, destabilize preformed filaments, or inhibit pathological seeding.<\/p>\n\n\n\n

Together, these efforts illustrate how complementary high-resolution techniques, XFEL-based SFX and cryo-EM, can be leveraged to investigate both essential biomolecular complexes and disease-relevant protein assemblies. Our findings contribute to structure-guided strategies for the development of new antibiotics and therapeutic approaches for ALS.<\/p>\n\n\n\n

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Click here to apply<\/a><\/h2>\n","protected":false},"excerpt":{"rendered":"

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