peptide cross-linking

Definition

Target type: biologicalprocess

The formation of a covalent cross-link between or within protein chains. [GOC:jsg]

Peptide cross-linking is a chemical process that covalently links two or more peptides together. This process can occur naturally within cells or be induced artificially in the lab. The resulting cross-linked peptides can form stable complexes that are resistant to enzymatic degradation. This makes them valuable tools for studying protein interactions and structures.

The process of peptide cross-linking can be divided into several steps. First, a cross-linking reagent is introduced to the system. This reagent typically contains two reactive groups that can react with amino acid residues on the peptides. The cross-linking reagent can be specific for certain amino acid residues, or it can be more promiscuous and react with a variety of residues.

Once the cross-linking reagent has been introduced, it can react with the peptides to form a cross-linked complex. The resulting cross-linked complex will be stabilized by the covalent bond between the peptides.

There are many different cross-linking reagents available, and each reagent has its own unique properties. Some reagents are more efficient at cross-linking peptides than others. Some reagents are more specific for certain amino acid residues than others. And some reagents are more stable than others.

Peptide cross-linking is a powerful tool that can be used to study protein interactions and structures. It can be used to identify new protein-protein interactions, to map protein-protein interfaces, and to study the dynamics of protein complexes.

In addition to its use in research, peptide cross-linking is also used in the development of new drugs and therapies. For example, cross-linking reagents are used to develop new antibiotics that target bacterial proteins.

The process of peptide cross-linking can be summarized as follows:

1. A cross-linking reagent is introduced to the system.
2. The cross-linking reagent reacts with amino acid residues on the peptides to form a cross-linked complex.
3. The resulting cross-linked complex is stabilized by the covalent bond between the peptides.

Peptide cross-linking is a versatile and powerful tool that has a wide range of applications in biology, chemistry, and medicine.'
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Proteins (3)

Compounds (19)