Microwave Dielectric Study on Unfolded Protein by Urea
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概要
- 論文の詳細を見る
Microwave dielectric measurements using a time domain reflectometry method were performed on a native α-chymotrypsin aqueous solution, a denatured α-chymotrypsin in 8M urea aqueous solution, and a denatured α-chymotrypsin in 1wt% mercaptoethanol-8M urea aqueous solution at 25℃. The bound water attached to biopolymers through hydrogen bonding reflected by dielectric relaxation process was observed for the native α-chymotrypsin aqueous solution. In the case of the denatured α-chymotrypsin unfolded by urea, micro-Brownian motions of the peptide chain were dominantly reflected by the relaxation process instead of the bound water. It is considered that the chain motion observed for the globular protein is an indication of unfolding caused by the denaturation.
- 東海大学の論文
著者
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HAYASHI Yoshihito
Department of Chemistry, Graduate School of Natural Science and Engineering, Kanazawa University
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YAGIHARA Shin
Department of Physics, Faculty of Science, Tokai University
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Yagihara S
Department Of Physics School Of Science Tokai University
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Yagihara Shin
Department Of Physics Faculty Of Science Tokai University
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Mikoshiba Masaaki
Department of Physics,School of Science,Tokai University
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Shinyashiki Naoki
Department of Physics,School of Science,Tokai University
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Hayashi Yoshihito
Department Of Chemistry Graduate School Of Natural Science And Technology
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Hayashi Yoshihito
Department Of Physics School Of Science Tokai University
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Mikoshiba Masaaki
Department Of Physics School Of Science Tokai University
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Shinyashiki N
Department Of Physics School Of Science Tokai University
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Shinyashiki Naoki
Department Of Physics School Of Science Tokai University
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Hayashi Yoshihito
Department Of Chemistry Division Of Material Sciences Graduate School Of Natural Science And Technology Kanazawa University
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