title: Comparative study of urea and betaine solutions by dielectric spectroscopy: liquid structures of a protein denaturant and stabilizer.
abstract: 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.
authors: Life Science Laboratory, Materials Laboratories, Sony Corporation, Sony Bioinformatics Center, Tokyo Medical and Dental University, Tokyo, Japan. yoshihito.hayashi@jp.sony.com
authors: Yoshihito
authors: Y
authors: Hayashi
authors: Yoichi
authors: Y
authors: Katsumoto
authors: Ikuya
authors: I
authors: Oshige
authors: Shinji
authors: S
authors: Omori
authors: Akio
authors: A
authors: Yasuda
mesh_terms: D001622:Betaine / Q000737:chemistry*; D004563:Electrochemistry; D011489:Protein Denaturation; D012996:Solutions; D013057:Spectrum Analysis; D014508:Urea / Q000737:chemistry*
chemical_list: D012996:Solutions; D001622:Betaine; D014508:Urea