書誌事項
- タイトル別名
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- Structural Reversibility of Protein by the use of a Hydrophilic Ionic Liquid; Chloline Dihydrogen Phosphate
- シン スイセイ イオン エキタイ Choline Dihydrogen Phosphate オ モチイタ タンパクシツ ノ Structural Reversibility
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We have investigated low temperature-induced structural reversibility of ribonuclease A (RNase A) in aqueous choline dihydrogen phoshpahte ([Chol][dhp]) solutions (X(mol%D_2O)=100〜70) by the uses of FTIR and Raman spectroscopies. From the IR spectral analyses, we found that the structural stability of RNase A remains unchanged in the concentration of [Chol][dhp] region from X=97 to 85. Moreover the secondary and tertiary structures of RNase A showed good reversibility upon cooling (77 K) in the same concentration region. On the other hand, Raman OD stretching spectra showed that the aqueous [Chol][dhp]-RNase A solutions take into the glassy state at 77 K in the region from X=90 to 70. On the basis of these results, in the concentration region from X=90 to 85, the aqueous [Chol][dhp]-RNase A solutions have a possibility of good cryoprospectant for aqueous protein solutions.
収録刊行物
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- 低温生物工学会誌
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低温生物工学会誌 58 (2), 147-151, 2012
低温生物工学会
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詳細情報 詳細情報について
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- CRID
- 1390282680064272768
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- NII論文ID
- 110009612928
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- NII書誌ID
- AN10448734
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- ISSN
- 24241555
- 13407902
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- NDL書誌ID
- 024143075
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可