Binding mechanism of Orange G to human serum albumin: Saturation transfer difference-NMR, spectroscopic and computational techniques

2013 ◽  
Vol 98 (2) ◽  
pp. 212-220 ◽  
Author(s):  
Ximin Zhou ◽  
Xi Li ◽  
Xingguo Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Computational Techniques ◽  
Binding Mechanism ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Orange G

scholarly journals Characterizing the interaction between methyl ferulate and human serum albumin by saturation transfer difference NMR

RSC Advances ◽  
2020 ◽  
Vol 10 (54) ◽  
pp. 32999-33009
Author(s):  
Wenjing Wang ◽  
Qiaomei Sun ◽  
Na Gan ◽  
Yuanming Zhai ◽  
Hongzhao Xiang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Saturation Transfer ◽  
Recognition Mechanism ◽  
Saturation Transfer Difference ◽  
Std Nmr ◽  
Methyl Ferulate

STD-NMR technique characterized the recognition mechanism of methyl ferulate and human serum albumin qualitatively and quantitatively.

scholarly journals Investigating the interaction mechanism of fluorescent whitening agents to human serum albumin using saturation transfer difference-NMR, multi-spectroscopy, and docking studies

RSC Advances ◽  
2017 ◽  
Vol 7 (44) ◽  
pp. 27796-27806 ◽  
Author(s):  
Ludan Zhao ◽  
Jiuyang Liu ◽  
Ronghui Guo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Interaction Mechanism ◽  
Docking Studies ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Fluorescent Whitening Agents ◽  
Std Nmr

Characterization of the interaction between two fluorescent whitening agents and human serum albumin: 1H STD-NMR, multi-spectroscopy, and docking studies.

Binding mechanism of tauroursodeoxycholic acid to human serum albumin: insights from NMR relaxation and docking simulations

RSC Advances ◽  
2015 ◽  
Vol 5 (15) ◽  
pp. 11036-11042 ◽  
Author(s):  
Di Wu ◽  
Yuanming Zhai ◽  
Jin Yan ◽  
Kailin Xu ◽  
Qing Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nmr Relaxation ◽  
Binding Mechanism ◽  
Tauroursodeoxycholic Acid ◽  
Docking Simulations ◽  
Relationship Of

Binding patterns and structure–affinity relationship of tauroursodeoxycholic acid with human serum albumin were established by NMR methodology and docking simulations.

Chromatographic Framework to Determine the Memantine Binding Mechanism on Human Serum Albumin Surface

2008 ◽  
Vol 68 (3-4) ◽  
pp. 179-186 ◽  
Author(s):  
Firas Ibrahim ◽  
Yves-Claude Guillaume ◽  
Claire André
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Mechanism
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