Related Experiment Video
Updated: Jul 6, 2026
12:11
Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
Chemical approaches to mapping the function of post-translational modifications
David P Gamblin1, Sander I van Kasteren, Justin M Chalker
1Chemistry Research Laboratory, Department of Chemistry, University of Oxford, UK.
The FEBS Journal
|April 4, 2008
Summary
Synthetic protein construction enables precise placement of modifications, aiding the study of protein function and proteome complexity. This chemical approach offers powerful insights into functional protein alterations.
Area of Science:
- Biochemistry
- Chemical Biology
- Proteomics
Background:
- Post-translational modifications (PTMs) are crucial for protein function and cellular regulation.
- Understanding the role of PTMs in complex proteomes is challenging due to their dynamic and diverse nature.
- Current methods for studying PTMs have limitations in precision and scope.
Purpose of the Study:
- To develop and showcase chemical strategies for synthesizing proteins with site-specific PTMs or their mimics.
- To provide a powerful tool for dissecting the functional impact of protein alterations.
- To advance the understanding of proteome complexity through precisely engineered protein models.
Main Methods:
- Chemical protein synthesis approaches.
- Site-specific incorporation of non-canonical amino acids or chemical mimics of PTMs.
- Characterization of synthetic proteins using biochemical and biophysical techniques.
Main Results:
- Demonstrated feasibility of chemically synthesizing proteins with precisely positioned PTM mimics.
- Enabled detailed investigation into the functional consequences of specific protein modifications.
- Provided a platform for dissecting the complexity of functional protein alteration.
Conclusions:
- Chemical synthesis of proteins with defined PTMs is a viable and powerful strategy.
- This approach offers unprecedented control for studying protein function and proteome complexity.
- The methodology facilitates deeper insights into the biological roles of protein modifications.
Related Concept Videos
02:04Covalently 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.
These groups modify specific amino acids in a protein.
01:02Phosphorylation
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...
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...