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- Kim, Chae Un
- High Pressure X-ray Science Lab.
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| DC Field | Value | Language |
|---|---|---|
| dc.citation.conferencePlace | KO | - |
| dc.citation.title | 2021년 대한금속재료학회 춘계학술대회 | - |
| dc.contributor.author | Kim, Chae Un | - |
| dc.date.accessioned | 2024-01-31T22:06:58Z | - |
| dc.date.available | 2024-01-31T22:06:58Z | - |
| dc.date.created | 2021-12-23 | - |
| dc.date.issued | 2021-04-21 | - |
| dc.description.abstract | Human carbonic anhydrase II (CA II) is a zinc metalloenzyme that catalyzes the reversible hydration/dehydration of CO2/HCO3 -. Although CA II has been extensively studied to investigate the proton-transfer process that occurs in the active site, its underlying mechanism is still not fully understood. In this presentation, we present the crystallographic structures of CA II using the High-pressure cryocrystallographic method. The structures reveal new intermediate solvent states of CA II that provide crystallographic snapshots during the restoration of the proton-transfer water network in the active site. In addition, the structures provide hints for the role of metal ions in CA II catalysis. |
- |
| dc.identifier.bibliographicCitation | 2021년 대한금속재료학회 춘계학술대회 | - |
| dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/77532 | - |
| dc.publisher | 대한금속재료학회 | - |
| dc.title | High-pressure Cryocrystallogrpahy for Metalloenzymes | - |
| dc.type | Conference Paper | - |
| dc.date.conferenceDate | 2021-04-28 | - |
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