Proteomics is the study of proteins, including their structure, function, and interactions.

Collagen is the most abundant protein in the human body, accounting for about 25% of total protein content.

Hemoglobin is a protein found in red blood cells that transports oxygen from the lungs to the rest of the body.

Proteomics can be used to identify new drug targets by studying the proteins involved in a particular disease process.

Mass spectrometry is the most common method used for protein identification. It involves ionizing proteins and measuring their mass-to-charge ratio.

Interactomics is the study of protein-protein interactions, including the identification of protein complexes and the mapping of protein interaction networks.

Gel electrophoresis is a technique used to separate proteins based on their size. It involves applying an electric field to a gel containing the proteins, which causes the proteins to migrate through the gel at different rates.

Post-translational modification is the process of modifying proteins after they have been synthesized. This can involve adding or removing chemical groups, cleaving the protein into smaller fragments, or changing the protein's conformation.

Western blotting is a technique used to detect and quantify proteins in a sample. It involves separating the proteins by gel electrophoresis, transferring them to a nitrocellulose membrane, and then incubating the membrane with antibodies specific to the proteins of interest.

Structural biology is the study of the structure and function of proteins. It involves using techniques such as X-ray crystallography and nuclear magnetic resonance spectroscopy to determine the three-dimensional structure of proteins.

Co-immunoprecipitation is a technique used to study the interactions between proteins and other molecules. It involves incubating a sample with an antibody specific to one of the molecules, and then immunoprecipitating the antibody-antigen complex. This allows the other molecules that interact with the antigen to be identified.

Proteomics can be used to study the role of proteins in disease by identifying the proteins that are differentially expressed or modified in diseased tissues.

The yeast two-hybrid assay is a technique used to identify the proteins that interact with a particular protein. It involves fusing the gene encoding the protein of interest to a DNA-binding domain, and then fusing the gene encoding a potential interacting protein to an activation domain. If the two proteins interact, they will bring the DNA-binding domain and the activation domain together, which will activate the transcription of a reporter gene.

Comparative proteomics is the study of the role of proteins in evolution. It involves comparing the proteomes of different species to identify proteins that are conserved or have diverged over time.