2010 Fiscal Year Final Research Report
Contribution of electrostatic interaction to thermo-stabilization of proteins from hyperthermophile
| Project/Area Number |
20589003
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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 |
Applied biochemistry
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
MATSUURA Yoshinori The Institute of Physical and Chemical Research, タンパク質結晶構造解析研究グループ, リサーチアソシエイト (50513462)
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| Project Period (FY) |
2008 – 2010
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| Keywords | 蛋白質の熱安定性 / 蛋白質工学 / 塩結合 / 超好熱菌 / 静電的相互作用 / イオン性アミノ酸 / CutA1 / DSC |
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| Research Abstract |
Proteins from hyperthermophiles contain a lot of ionic residues compared to those from other sources growing in moderate environments. However, the contribution of ionic interaction to thermo-stability of the proteins remains to be clearly understood. The CutA1 protein from hyperthermophile, Pyrococcus horikoshii (PhCutA1) shows the highest denaturation temperature of nearly 150 oC. In this report, we investigated the thermo-stabilities of more than 50 PhCutA1 mutants (from ionic to non-ionic residues) to elucidate the contribution of the ionic interaction.
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[Journal Article] High-throughput crystallization-to-structure pipeline at RIKEN SPring-8 Center2008
Author(s)
M.Sugahara, Y.Asada, K.Shimizu, H.Yamamoto, N.K.Lokanath, H Mizutani, B.Bagautdinov, Y Matsuura, M.Taketa, Y.Kageyama, N.Ono, Y.Morikawa, Y.Tanaka, H.Shimada, T.Nakamoto, M.Sugahara, M.Yamamoto, N.Kunishima
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Journal Title
J.Struct.Fund Genomics 9
Pages: 21-28
Peer Reviewed
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