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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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.

Labeling DNA Probes

Labeling DNA Probes

DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...

Phosphorylation

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...

Protein Kinases and Phosphatases

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...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: Jun 9, 2026

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

Probing protein function by chemical modification.

Yao-Wen Wu¹, Roger S Goody

¹Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany. wu@mpi-dortmund.mpg.de

Journal of Peptide Science : an Official Publication of the European Peptide Society

|September 4, 2010

Summary

This summary is machine-generated.

Protein labeling with synthetic probes aids in understanding protein function. This review covers chemical methods for site-specific protein modification and their biological applications.

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Area of Science:

Biochemistry
Chemical Biology
Molecular Biology

Background:

Protein labeling is crucial for studying protein function in various biological contexts.
Advancements in chemical synthesis have expanded the repertoire of available protein modification tools.

Purpose of the Study:

To review important chemical methods for site-specific protein modification.
To highlight the application of established techniques in addressing biological questions.

Main Methods:

Discussion of chemical strategies for protein labeling.
Review of established techniques for site-specific protein modification.

Main Results:

Overview of diverse synthetic probes including fluorophores and affinity tags.
Demonstration of how these methods enable detailed characterization of protein function.
Examples of applying these techniques to solve biological problems.

Conclusions:

Site-specific protein modification is a powerful approach in biological research.
Chemical methods provide versatile tools for protein characterization and functional studies.