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.

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 Unveiling the Interaction of Vanadium Compounds with Human Serum Albumin by Using1H STD NMR and Computational Docking Studies

2013 ◽  
Vol 2013 (26) ◽  
pp. 4619-4627 ◽  
Author(s):  
David M. Dias ◽  
João P. G. L. M. Rodrigues ◽  
Neuza S. Domingues ◽  
Alexandre M. J. J. Bonvin ◽  
M. Margarida C. A. Castro
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Studies ◽  
Vanadium Compounds ◽  
Computational Docking ◽  
Std Nmr

Characterization of the interaction between acotiamide hydrochloride and human serum albumin: 1H STD NMR spectroscopy, electrochemical measurement, and docking investigations

RSC Advances ◽  
2016 ◽  
Vol 6 (66) ◽  
pp. 61119-61128 ◽  
Author(s):  
Jiawei He ◽  
Hongqin Yang ◽  
Shanshan Li ◽  
Kailin Xu ◽  
Qing Wang ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrochemical Measurement ◽  
Binding Mechanism ◽  
Comprehensive Investigation ◽  
Std Nmr

The comprehensive investigation of acotiamide hydrochloride and HSA interaction provides a convictive explanation for its binding mechanism.

scholarly journals Characterization of the Solution Structure of Human Serum Albumin Loaded with a Metal Porphyrin and Fatty Acids

2011 ◽  
Vol 100 (9) ◽  
pp. 2293-2301 ◽  
Author(s):  
Matthias J.N. Junk ◽  
Hans W. Spiess ◽  
Dariush Hinderberger
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solution Structure ◽  
Metal Porphyrin

Highly precise characterization of the hydration state upon thermal denaturation of human serum albumin using a 65 GHz dielectric sensor

2020 ◽  
Vol 22 (35) ◽  
pp. 19468-19479 ◽  
Author(s):  
Keiichiro Shiraga ◽  
Mako Urabe ◽  
Takeshi Matsui ◽  
Shojiro Kikuchi ◽  
Yuichi Ogawa
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermal Denaturation ◽  
Hydration Water ◽  
Biological Functions ◽  
Dielectric Sensor ◽  
Hydration State ◽  
Precise Characterization

The biological functions of proteins depend on harmonization with hydration water surrounding them.

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