The effect of surface coverage on conformation changes of bovine serum albumin molecules at the air–solution interface detected by sum frequency generation vibrational spectroscopy

The Analyst ◽  
2003 ◽  
Vol 128 (6) ◽  
pp. 773-778 ◽  
Author(s):  
Jie Wang ◽  
Sarah M. Buck ◽  
Zhan Chen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Vibrational Spectroscopy ◽  
Bovine Serum ◽  
Surface Coverage ◽  
Sum Frequency Generation ◽  
Sum Frequency ◽  
Solution Interface ◽  
Conformation Changes ◽  
Effect Of Surface

Influence of Terahertz Radiation of Various Ranges on Molecule Conformation of Bovine Serum Albumin

2010 ◽  
Vol 5 (4) ◽  
pp. 182-185
Author(s):  
Angelina V. Kapralova ◽  
Aleksandr S. Pogodin
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Radiation Power ◽  
Uv Spectrophotometry ◽  
Absorption Bands ◽  
Conformation Changes ◽  
Protein Molecules ◽  
Molecule Conformation ◽  
Protein Bovine Serum Albumin

We investigated the influence of THz laser radiation of frequencies of 1.15 THz and 3.68 THz and radiation power of about 10 Mw on protein (bovine serum albumin). Using UV spectrophotometry, we revealed increase in the optical density of irradiated samples of bovine serum albumin at the characteristic absorption bands, which is evidence of conformation changes in protein molecules

Spectroscopic study of conformation changes of bovine serum albumin in aqueous environment

2019 ◽  
Vol 30 (6) ◽  
pp. 1302-1306 ◽  
Author(s):  
Chune Guo ◽  
Xiaomi Guo ◽  
Wubo Chu ◽  
Nan Jiang ◽  
He Li
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Spectroscopic Study ◽  
Bovine Serum ◽  
Aqueous Environment ◽  
Conformation Changes

Effect of surface charge on adsorption of bovine serum albumin as studied by ellipsometry 1. Adsorption on cationic monolayer

1986 ◽  
Vol 264 (10) ◽  
pp. 903-908 ◽  
Author(s):  
N. Watanabe ◽  
T. Shirakawa ◽  
M. Iwahashi ◽  
K. Ohbu ◽  
T. Seimiya
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Charge ◽  
Bovine Serum ◽  
Effect Of Surface

scholarly journals Interaction of Conazole Pesticides Epoxiconazole and Prothioconazole with Human and Bovine Serum Albumin Studied Using Spectroscopic Methods and Molecular Modeling

2021 ◽  
Vol 22 (4) ◽  
pp. 1925
Author(s):  
Katarína Golianová ◽  
Samuel Havadej ◽  
Valéria Verebová ◽  
Jozef Uličný ◽  
Beáta Holečková ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Association Constants ◽  
Van Der Waals Interactions ◽  
Spectroscopic Methods ◽  
Spectroscopic Techniques ◽  
Conformation Changes

The interactions of epoxiconazole and prothioconazole with human serum albumin and bovine serum albumin were investigated using spectroscopic methods complemented with molecular modeling. Spectroscopic techniques showed the formation of pesticide/serum albumin complexes with the static type as the dominant mechanism. The association constants ranged from 3.80 × 104–6.45 × 105 L/mol depending on the pesticide molecule (epoxiconazole, prothioconazole) and albumin type (human or bovine serum albumin). The calculated thermodynamic parameters revealed that the binding of pesticides into serum albumin macromolecules mainly depended on hydrogen bonds and van der Waals interactions. Synchronous fluorescence spectroscopy and the competitive experiments method showed that pesticides bind to subdomain IIA, near tryptophan; in the case of bovine serum albumin also on the macromolecule surface. Concerning prothioconazole, we observed the existence of an additional binding site at the junction of domains I and III of serum albumin macromolecules. These observations were corroborated well by molecular modeling predictions. The conformation changes in secondary structure were characterized by circular dichroism, three-dimensional fluorescence, and UV/VIS absorption methods.

Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex

2015 ◽  
Vol 6 (8) ◽  
pp. 2712-2726 ◽  
Author(s):  
Xin Peng ◽  
Xiangchao Wang ◽  
Wei Qi ◽  
Renliang Huang ◽  
Rongxin Su ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Rosmarinic Acid ◽  
Acid Complex ◽  
Conformation Changes ◽  
Naturally Occurring

Rosmarinic acid (RA) is an importantly and naturally occurring polyphenol. The interaction between bovine serum albumin and rosmarinic acid was studied to investigate the binding patterns and conformation changes.

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