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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
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Identification of Phosphorylated Proteins on a Global Scale
1Tymora Analytical Operations, Innovations, West Lafayette, Indiana.
Current Protocols in Chemical Biology
|June 22, 2018
Summary
Liquid chromatography-tandem mass spectrometry (LC-MS/MS) advances proteomic analysis of complex biological samples. This study details effective sample preparation methods for phosphoproteomic experiments, focusing on phosphorylation analysis.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Molecular Biology
Background:
- Liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) offers deep analysis of biological samples.
- Proteomic experiments can identify and quantify thousands of protein modifications.
- Phosphorylation is a key post-translational modification crucial for cellular processes.
Purpose of the Study:
- To provide detailed protocols for sample preparation in phosphoproteomic studies.
- To enhance the effectiveness of phosphoproteomic experiments.
- To support researchers in analyzing phosphorylation in complex biological systems.
Main Methods:
- Liquid chromatography (LC) coupled with tandem mass spectrometry (MS/MS).
- Sample preparation techniques for phosphoproteomics.
- Identification and quantification of protein phosphorylation.
Main Results:
- Established protocols enable in-depth analysis of complex biological samples.
- Facilitated identification and quantification of numerous protein modifications.
- Demonstrated progress in analyzing phosphorylation using advanced LC-MS/MS techniques.
Conclusions:
- Advanced LC-MS/MS methods significantly improve proteomic analysis.
- Effective sample preparation is critical for successful phosphoproteomic studies.
- The provided protocols support robust analysis of phosphorylation events.
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