Fluorescence spectroscopy and molecular simulation on the interaction of caffeic acid with human serum albumin

Luminescence ◽  
2016 ◽  
Vol 31 (8) ◽  
pp. 1496-1502 ◽  
Author(s):  
Yuhong Xiang ◽  
Lili Duan ◽  
Qiang Ma ◽  
Zizheng Lv ◽  
Zhu Ruohua ◽  
...  
2011 ◽  
Vol 27 (1) ◽  
pp. 79-84 ◽  
Author(s):  
Feng GE ◽  
Lixiang JIANG ◽  
Diqiu LIU ◽  
Chaoyin CHEN

Author(s):  
Ali Jahanban-Esfahlan ◽  
Leila Roufegarinejad ◽  
Mahnaz Tabibiazar ◽  
José Lorenzo ◽  
Ryszard Amarowicz

2020 ◽  
Vol 54 (3 (253)) ◽  
pp. 261-264
Author(s):  
M.A. Shahinyan ◽  
N.H. Petrosyan ◽  
A.P. Antonyan

The interaction of methyl violet (MV) with human serum albumin (HSA) has been studied, using the fluorescence spectroscopy method. It was shown that MV chnages the own fluorescence of HSA. It was also shown that MV does not induce any conformational change in the structure of HSA, since there is no change of the wavelength of HSA fluorescence intensity maximum. MV binds to HSA, near to fluorescing tryptophan, which in the hydrophilic environment, and changes the own fluorescence of the protein.


2006 ◽  
Vol 22 (12) ◽  
pp. 1456-1459
Author(s):  
LIU Yong-Ming ◽  
◽  
◽  
LI Gui-Zhi ◽  
SONG Wan-Kun ◽  
...  

RSC Advances ◽  
2016 ◽  
Vol 6 (94) ◽  
pp. 91756-91767 ◽  
Author(s):  
Md. Zahirul Kabir ◽  
Wei-Ven Tee ◽  
Saharuddin B. Mohamad ◽  
Zazali Alias ◽  
Saad Tayyab

Binding orientation of the GEF in the binding site III, located in subdomain IB of HSA.


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