Investigation on the conformational changes of bovine serum albumin in a wide pH range from 2 to 12
Author:
Affiliation:
1. School of Marine Science and Technology, Harbin Institute of Technology, Weihai, PR China;
2. Guangzhou Key Laboratory of Environmental Exposure and Health, School of Environment, Jinan University, Guangzhou, PR China
Funder
National Natural Science Foundation of China
the Guangzhou Key Laboratory of Environmental Exposure and Health
the Shandong Provincial Natural Science Foundation, China
The Natural Scientific Research Innovation Foundation in Harbin Institute of Technology
Publisher
Informa UK Limited
Subject
Spectroscopy,Atomic and Molecular Physics, and Optics,Analytical Chemistry
Link
https://www.tandfonline.com/doi/pdf/10.1080/00387010.2018.1471092
Reference36 articles.
1. Binding of amifostine to human serum albumin: A biophysical study
2. Unraveling the binding mechanism of asiatic acid with human serum albumin and its biological implications
3. Enhancement of cell uptake and antitumor activity of selenadiazole derivatives through interaction and delivery by serum albumin
4. Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex
5. Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin
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