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Conformational Change of Bovine Serum Albumin Molecules at Neutral pH in Ultra-Diluted Aqueous Solutions

โœ Scribed by He, Shulian; Huang, Mei; Ye, Wei; Chen, Dechao; He, Shuai; Ding, Liping; Yao, Yunjin; Wan, Lei; Xu, Jinzhang; Miao, Shiding


Book ID
126561586
Publisher
American Chemical Society
Year
2014
Tongue
English
Weight
692 KB
Volume
118
Category
Article
ISSN
0022-3654

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Conformational Changes of Bovine Serum A
โœ Kunio Takeda; Kazumasa Harada; Kouji Yamaguchi; Yoshiko Moriyama ๐Ÿ“‚ Article ๐Ÿ“… 1994 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 284 KB

The helicity of bovine serum albumin (BSA) decreased both in the reverse micelle of sodium bis(2-ethylhexyl) sulfosuccinate (AOT) and in the aqueous solution of the same surfactant (the saturated binding amount to the protein was \(70 \mathrm{~mol} / \mathrm{mol}\) ). In both cases, the final helici