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Related Concept Videos

Phosphorylation01:02

Phosphorylation

44.6K
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...
44.6K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

12.1K
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...
12.1K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.2K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.2K
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

15.4K
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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Related Experiment Video

Updated: Apr 24, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

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Site-specifically phosphorylated lysine peptides.

Jordi Bertran-Vicente1, Remigiusz A Serwa, Michael Schümann

  • 1Leibniz-Institut für Molekulare Pharmakologie (FMP) , Robert-Rössle Str. 10, 13125 Berlin, Germany.

Journal of the American Chemical Society
|September 9, 2014
PubMed
Summary

Researchers developed a new method for synthesizing phospholysine peptides, enabling the study of lysine phosphorylation. This breakthrough facilitates the detection and biological relevance evaluation of this crucial post-translational modification.

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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Protein phosphorylation is vital for cellular processes, with lysine phosphorylation's role being largely unexplored.
  • Existing methods are limited by the instability of phospholysine during peptide synthesis.

Purpose of the Study:

  • To develop a novel synthetic route for site-specific phospholysine (pLys)-containing peptides.
  • To enable the study of lysine phosphorylation's biological significance.

Main Methods:

  • Utilized the Staudinger-phosphite reaction for chemoselective synthesis.
  • Employed solid-phase peptide synthesis (SPPS) with azido lysine peptides.
  • Converted phosphoramidates to pLys via UV irradiation or basic deprotection.

Main Results:

  • Successfully synthesized site-specifically pLys-containing peptides.
  • Demonstrated electron-transfer dissociation tandem mass spectrometry for pLys assignment in histone peptides.
  • Showcased detection of these peptides in cell lysates using bottom-up proteomics.

Conclusions:

  • The new synthetic method overcomes previous limitations in studying lysine phosphorylation.
  • This approach is crucial for investigating the biological relevance of lysine phosphorylation.
  • The developed technique is expected to be an essential tool in the field.