H/D Isotope Effects in Protein Thermal Denaturation: The Case of Bovine Serum Albumin

2011 ◽  
Vol 115 (8) ◽  
pp. 1881-1888 ◽  
Author(s):  
Ling Fu ◽  
Sandrine Villette ◽  
Stéphane Petoud ◽  
Felix Fernandez-Alonso ◽  
Marie-Louise Saboungi
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation ◽  
Isotope Effects

Thermal denaturation of bovine serum albumin and its oligomers and derivativespH dependence

1995 ◽  
Vol 45 (6) ◽  
pp. 1255-1264 ◽  
Author(s):  
G. Barone ◽  
S. Capasso ◽  
P. Del Vecchio ◽  
C. De Sena ◽  
D. Fessas ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation

BOVINE SERUM ALBUMIN DENATURATION IN THE PRESENCE OF HOECHST 33258 AND METHYLENE BLUE

2020 ◽  
Vol 54 (3 (253)) ◽  
pp. 204-208
Author(s):  
P.O. Vardevanyan ◽  
M.S. Mikaelyan ◽  
N.H. Petrosyan
Keyword(s):  
Methylene Blue ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation ◽  
Native Structure ◽  
Hoechst 33258 ◽  
Denaturation Temperature

The interaction of Hoechst 33258 (H33258) and methylene blue (MB) compounds with bovine serum albumin (BSA) has been studied using the method of thermal denaturation. The obtained data showed that both ligands form complexes with BSA, moreover, MB binds to BSA stronger than H33258. Furthermore, H33258 destabilizes, while MB stabilizes the native structure of protein, leading to the decrease and increase of the denaturation temperature of BSA respectively.

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