Comparative Study of Urea and Betaine Solutions by Dielectric Spectroscopy: Liquid Structures of a Protein Denaturant and Stabilizer

We performed dielectric spectroscopy measurements on aqueous solutions of glycine betaine (N,N,N-trimethylglycine), which is known to be a strong stabilizer of globular proteins, over a wide concentration range (3−62 wt %) and compared the results with our previously published data for aqueous solut...

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Veröffentlicht in:	The journal of physical chemistry. B 2007-10, Vol.111 (40), p.11858-11863
Hauptverfasser:	Hayashi, Yoshihito, Katsumoto, Yoichi, Oshige, Ikuya, Omori, Shinji, Yasuda, Akio
Format:	Artikel
Sprache:	eng
Schlagworte:	Betaine - chemistry Electrochemistry Protein Denaturation Solutions Spectrum Analysis Urea - chemistry
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container_end_page	11863
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container_title	The journal of physical chemistry. B
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creator	Hayashi, Yoshihito Katsumoto, Yoichi Oshige, Ikuya Omori, Shinji Yasuda, Akio
description	We performed dielectric spectroscopy measurements on aqueous solutions of glycine betaine (N,N,N-trimethylglycine), which is known to be a strong stabilizer of globular proteins, over a wide concentration range (3−62 wt %) and compared the results with our previously published data for aqueous solutions of urea, a representative protein denaturant. The hydration number of betaine (9), calculated on the basis of the reduction in the dielectric relaxation strength of bulk water with addition of betaine, is significantly larger than that of urea (2). Furthermore, the dielectric relaxation time increased with betaine concentration, while that remained nearly constant for the urea−water system over a wide concentration range. This difference between urea and betaine is probably related to their opposite effects on the protein stabilization.
doi_str_mv	10.1021/jp073238j
format	Article
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subjects	Betaine - chemistry Electrochemistry Protein Denaturation Solutions Spectrum Analysis Urea - chemistry
title	Comparative Study of Urea and Betaine Solutions by Dielectric Spectroscopy: Liquid Structures of a Protein Denaturant and Stabilizer
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