Related Experiment Video
Updated: Jun 21, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
Study on the interaction between methyl violet and bovine serum albumin by spectral analyses
Yanyan Hu1, Suqin Xu, Xiashi Zhu
1Department of Chemistry, Yangzhou University, Yangzhou 225002, Jiangsu, PR China.
Abstract:
In this article the interaction between methyl violet (MV) and bovine serum albumin (BSA) was studied with spectroscopy. The results indicated that the fluorescence intensity of BSA was quenched strongly by MV through a static quenching procedure. The association constants, the number of binding sites and basic thermodynamic parameters were obtained based on fluorescence quenching data. The effect of MV on the conformation of BSA had been investigated with synchronous fluorescence spectroscopy and circular dichroism (CD) spectrum.
Related Concept Videos
UV–Vis Spectroscopy: Beer–Lambert Law
UV–Vis Spectroscopy of Conjugated Systems
One of the factors influencing λmax is the extent of conjugation in the...
Spectrophotometry: Introduction
The essential components of a spectrophotometer include a source of electromagnetic radiation, a slot for placing a material to be analyzed, and a...
Estimation of k and VD of Aminoglycosides
IR and UV–Vis Spectroscopy of Aldehydes and Ketones
