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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...

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Related Experiment Video

Updated: Jul 10, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

A 2D NMR method to study peptide phosphorylation.

Christian Raeck1, Stefan Berger

  • 1Institute of Analytical Chemistry, University of Leipzig, Linnéstr. 3, Leipzig, 04103, Germany.

Analytical and Bioanalytical Chemistry
|October 24, 2007
PubMed
Summary

This study introduces a novel 2D NMR technique to differentiate phosphorylated from non-phosphorylated amino acids. This method enables precise monitoring of enzymatic phosphorylation and dephosphorylation in peptides.

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Oligopeptide Competition Assay for Phosphorylation Site Determination
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A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
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A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

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Last Updated: Jul 10, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
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A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Spectroscopy

Background:

  • Phosphorylation is a critical post-translational modification regulating protein function.
  • Monitoring site-specific phosphorylation dynamics is essential for understanding cellular processes.

Purpose of the Study:

  • To develop a 2D Nuclear Magnetic Resonance (NMR) method for distinguishing phosphorylated and non-phosphorylated amino acids.
  • To enable site-specific monitoring of enzymatic phosphorylation and dephosphorylation in peptides.

Main Methods:

  • Utilized a novel 2D NMR approach.
  • Developed the method using O-phosphorylated amino acids.
  • Applied the technique to a peptide fragment of myelin basic protein (MBP).

Main Results:

  • Successfully demonstrated the ability to distinguish between phosphorylated and non-phosphorylated amino acids.
  • Showcased the method's capability for monitoring enzymatic phosphorylation and dephosphorylation at specific amino acid sites within peptides.

Conclusions:

  • The developed 2D NMR method provides a powerful tool for analyzing phosphorylation dynamics.
  • This technique offers potential for detailed studies of enzyme activity and post-translational modifications in complex biological systems.