Related Experiment Video
Updated: Aug 29, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
Published on: June 19, 2010
The nature of phosphorylated chrysin-protein interactions involved in noncovalent complex formation by electrospray
Xiao-Lan Chen1, Ling-Bo Qu, Ting Zhang
1Department of Chemistry, Key Laboratory of Chemical Biology, Zhengzhou University, Zhengzhou, 450052, PR China.
Abstract:
In the work described in this paper, chrysin was phosphorylated by a modified Atheron-Todd reaction. The structure of phosphorylated chrysin was determined by elemental analysis, NMR, ESI-MS/MS, and X-ray data. Electrospray ionization results showed that the phosphorylated flavonoids could form noncovalent complexes with many proteins, such as lysozyme, myoglobin, bovine insulin, and cytochrome c, while noncovalent complexes were not detected in the mixed solution of the chrysin and proteins. The research shows that the phosphorylated flavonoids possess relatively stronger affinities and form noncovalent complexes with the proteins more easily than the non-phosphorylated compounds.
More Related Videos
09:18Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
Published on: April 17, 2017
12:47Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Related Concept Videos
Electrospray Ionization (ESI) Mass Spectrometry
ESI utilizes electrical energy to transfer ions from the liquid phase of the sample into the...
Inductively Coupled Plasma-Mass Spectrometry (ICP-MS): Interferences
Mass Spectrometry: Complex Analysis
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...