2011 Fiscal Year Final Research Report
Structural analysis of the transient state of an enzyme active site using NMR relaxation dispersion
| Project/Area Number |
21570170
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Osaka University |
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Principal Investigator |
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| Project Period (FY) |
2009 – 2011
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| Keywords | 核磁気共鳴 / NMR / 遷移状態 / induced-fit / 構造解析 |
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| Research Abstract |
An enzyme chitinase was aligned along the static magnetic field using Pf1-phage or acrylamide gel as an alignment medium. In this state residual dipolar coupling was observed, confirming that the system was effective for the analysis. To further apply the relaxation dispersion method to the alignment system, a complex system which was well known to be in a conformational exchange was used. Upon changing the stoichiometry in the complex, it was observed that the residual dipolar coupling also changed accordingly.
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[Journal Article] Binding Energetics of Ferredoxin-NADP^+ Reductase with Ferredoxin and Its Relation to Function2011
Author(s)
Lee, Y. H., Ikegami, T., Standley, D. M., Sakurai, K., Hase, T., and Goto, Y.
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Journal Title
Chembiochem
Volume: 12
Pages: 2062-2070
Peer Reviewed
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