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氷/水界面への不凍糖タンパク質分子の吸着と拡散
https://jaxa.repo.nii.ac.jp/records/13500
https://jaxa.repo.nii.ac.jp/records/13500917b1878-ff44-4a64-a2c9-d0724379ff41
名前 / ファイル | ライセンス | アクション |
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63349002.pdf (513.2 kB)
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Item type | 会議発表論文 / Conference Paper(1) | |||||
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公開日 | 2015-03-26 | |||||
タイトル | ||||||
タイトル | 氷/水界面への不凍糖タンパク質分子の吸着と拡散 | |||||
言語 | ||||||
言語 | jpn | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | タンパク質 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 吸着 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 拡散 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | タンパク質結晶成長 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 結晶成長 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 不凍タンパク質 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 不凍糖タンパク質 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 氷-水界面 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 共焦点顕微鏡 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 氷結晶 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 蛍光 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 過冷却 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 赤外分光法 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 結晶構造 | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | protein | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | adsorption | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | diffusion | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | protein crystal growth | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | crystal growth | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | antifreeze protein | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | antifreeze glycoprotein | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | ice/water interface | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | confocal microscope | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | ice crystal | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | fluorescence | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | supercooling | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | infrared spectroscopy | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | crystal structure | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_5794 | |||||
資源タイプ | conference paper | |||||
その他のタイトル(英) | ||||||
その他のタイトル | Adsorption and diffusion of Antifreeze Glycoprotein molecules at ice/water interface | |||||
著者 |
古川, 義純
× 古川, 義純× Zepeda, Salvador× 宇田, 幸弘× 中谷, 浩之× 横山, 悦郎× Furukawa, Yoshinori× Zepeda, Salvador× Uda, Yukihiro× Nakaya, Hiroyuki× Yokoyama, Etsuro |
|||||
著者所属 | ||||||
北海道大学低温科学研究所 | ||||||
著者所属 | ||||||
北海道大学低温科学研究所 | ||||||
著者所属 | ||||||
北海道大学低温科学研究所 | ||||||
著者所属 | ||||||
北海道大学低温科学研究所 | ||||||
著者所属 | ||||||
学習院大学 計算機センター | ||||||
著者所属(英) | ||||||
en | ||||||
Institute of Low Temperature Science, Hokkaido University | ||||||
著者所属(英) | ||||||
en | ||||||
Institute of Low Temperature Science, Hokkaido University | ||||||
著者所属(英) | ||||||
en | ||||||
Institute of Low Temperature Science, Hokkaido University | ||||||
著者所属(英) | ||||||
en | ||||||
Institute of Low Temperature Science, Hokkaido University | ||||||
著者所属(英) | ||||||
en | ||||||
Gakushuin University Computer Center | ||||||
出版者 | ||||||
出版者 | 宇宙航空研究開発機構宇宙科学研究本部 | |||||
出版者(英) | ||||||
出版者 | Institute of Space and Astronautical Science, Japan Aerospace Exploration Agency (JAXA/ISAS) | |||||
書誌情報 |
宇宙利用シンポジウム 第23回 平成18年度 en : Space Utilization Research: Proceedings of the Twenty-third Space Utilization Symposium p. 5-8, 発行日 2007-03 |
|||||
抄録(英) | ||||||
内容記述タイプ | Other | |||||
内容記述 | Antifreeze Proteins (AFPs) and Glycoproteins (AFGPs) are found in nature in many cold weather organisms including fish, amphibians, plants and insects. These proteins suppress the freezing temperature of the blood serum in fish just enough to keep them from freezing in their supercooled environments while the melting temperature remains unchanged (hysteresis) and inhibit ice recrystallization enough to reduce damage in freeze tolerant organisms, making them essential for survival. To date workers have described at least five distinct classes of these proteins, AFP types 1 to 4 and AFGPs, as well as two distinct types of insect AFPs. The Type 1 and Type 2 AFPs are alanine and cysteine rich, respectively, while the AFGPs are alanine rich as well as glycosolated. They exist in a variety of structures ranging from alpha- or beta-helical to globular and yet to some extent they all accomplish the same function. These proteins are thought to bind to the surface of ice and inhibit growth. Although, this mechanism has recently been challenged by mutation experiments, where the residues thought to bind to the ice lattice were replaced with hydrophobic ones and these retained nearly all of the antifreeze activity. However, there is a consensus that this is a surface phenomenon, but no clear evidence for the exact nature of the mechanism is available and is necessary to understand how these proteins work. In this work, we use 3-d confocal microscopy to gain insight into the antifreeze interaction with the ice/solution interface. Single ice crystals are grown in solution from a capillary in the presence of antifreeze proteins labeled with Fluorescein Isothiocyanate (FITC). At 5 micro-g/ml quantities of AFGP we see a clear adsorption at the prismatic planes with growth stopped while the temperature is in the hysteresis region. When we lower the temperature below the hysteresis region growth continues while the protein is rejected from the crystal. At higher concentrations the gross morphology can vary quite dramatically, but the proteins are still rejected from the solid. This contradicts previous understandings that the mechanism for antifreeze action must be a tight irreversible binding. Furthermore, the conformational change of Antifreeze Glycoprotein (AFGP) molecules during ice formation on the AFGP thin film was followed by Attenuated Total Reflection (ATR)-FTIR (Fourier Transform Infrared) spectroscopy. The ATR-FTIR difference spectrum of the frozen and supercooled samples showed that helical conformation of AFGP molecules is predominant at the ice-water interface. | |||||
資料番号 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 資料番号: AA0063349002 |