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Protein chemical modification on endogenous amino acids
Emmanuel Baslé1, Nicolas Joubert, Mathieu Pucheault
1Molecular Chemistry and Photonic, UMR 6510 CPM, Centre National de la Recherche Scientifique, Université de Rennes1, 263 Avenue du Général Leclerc, 35042 Rennes cedex, France.
Chemistry & Biology
|March 27, 2010
Summary
This review explores chemical modifications for proteins, detailing selective reactions. Applications include protein interaction detection, bioconjugate preparation, and protein microarrays for biological research.
Area of Science:
- Biochemistry
- Organic Chemistry
- Molecular Biology
Background:
- Chemical modification of proteins is essential for various biological applications.
- Developing selective and reactive chemical methods is crucial for successful protein modification.
- A wide array of tools exists for chemists and biologists to modify proteins.
Purpose of the Study:
- To review diverse chemical transformations for selective protein modification.
- To highlight key applications of these chemical modification techniques.
- To provide insights into the strategic selection of reactions for protein manipulation.
Main Methods:
- Literature review of chemical modification strategies for proteins.
- Categorization of chemical reactions based on selectivity and reactivity.
- Analysis of applications in bioconjugation, interaction studies, and microarray development.
Main Results:
- Detailed overview of various selective chemical modification reactions for proteins.
- Examples of successful applications in detecting protein interactions.
- Demonstration of utility in preparing bioconjugates and constructing protein microarrays.
Conclusions:
- Selective chemical modification offers powerful tools for biological research.
- The choice of chemical method depends on the specific application and desired outcome.
- These techniques are vital for advancing fields like proteomics and diagnostics.
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.
01:26Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
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...
01:25Protein Glycosylation
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
03:42Amino acids
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
01:28What are Proteins?
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight. Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional structure...