Anion-induced refolding of human serum albumin under low pH conditions
โ Scribed by Salman Muzammil; Yogesh Kumar; Saad Tayyab
- Book ID
- 114150079
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 314 KB
- Volume
- 1476
- Category
- Article
- ISSN
- 0167-4838
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๐ SIMILAR VOLUMES
Small-angle X-ray scattering (SAXS) was used to study structural characteristics of human serum albumin (HSA) in solution under different pH conditions. Guinier analysis of SAXS results yielded values of the molecular radius of gyration ranging from 26.7 A to 34.5 A for pH varying from 2.5 to 7.0. T
The unfolding of human serum albumin (HSA), a multidomain protein, by urea was followed by far-UV circular dichroism (CD), intrinsic fluorescence, and ANS fluorescence measurements. The urea-induced transition, which otherwise was a two-step process with a stable intermediate at around 4.8 M urea co