2015 Fiscal Year Final Research Report
Study of aromatic ring-flipping in protein interiors at high pressures
Project/Area Number |
25440018
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
|
Research Institution | Kumamoto University (2015) Nagoya University (2013-2014) |
Principal Investigator |
|
Project Period (FY) |
2013-04-01 – 2016-03-31
|
Keywords | NMR / SAIL |
Outline of Final Research Achievements |
The side-chain aromatic rings of phenylalanine and tyrosine residues in the interior of protein frquenty rotate about their Cb-Cg axis, which is assumed to occur when the protein undergoes a large amplitude slow breathing motion. In this project, uder varied hydrotatic pressures, the ring flipping rates were evaluated by using the SAIL-NMR methds. This study expectedly provides new insight into the large amplitude motion of proteins.
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Free Research Field |
構造生物化学
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