Protein post-translational modification (PTM) increases the functional diversity of the proteome by covalently adding functional groups or proteins, proteolytic cleavage of regulatory subunits, or degradation of the entire protein. These modifications include phosphorylation, glycosylation, ubiquitination, nitrosylation, methylation, acetylation, lipidation and proteolysis, and affect almost all aspects of normal cell biology and pathogenesis. Therefore, the identification and understanding of PTM is crucial to the research of cell biology and disease treatment and prevention. Protein post-translational modification (PTM) has further contributed to the increase in complexity from the genomic level to the proteomic level. PTMs are chemical modifications that play a key role in functional proteomics because they regulate activity, localization, and interaction with other cellular molecules such as proteins, nucleic acids, lipids, and cofactors.
In recent years, high-throughput experimental methods based on mass spectrometry have been developed and are becoming more and more popular. In addition, PTM computational modeling represents another attractive method with its accuracy, speed and convenience. CD ComputaBio uses computational models to predict potential PTM sites in proteins, and models the side chain and main chain conformations to reflect changes caused by common PTMs. Our algorithm has been trained using existing PTMs observed in the protein database and proved to be fast and accurate.
|Post-translational modification service
Reversible protein phosphorylation, mainly on serine, threonine or tyrosine residues, is the most important and well-studied kind of post-translational modification. Phosphorylation plays a key role in the regulation of many cellular processes, including cell cycle, growth, apoptosis and signal transduction pathways.
Protein glycosylation is considered to be one of the main post-translational modifications, which has a significant impact on protein folding, conformation, distribution, stability and activity.
Ubiquitin is an 8 kDa polypeptide composed of 76 amino acids, which is attached to the α-NH2 of the lysine in the target protein through the C-terminal glycine of ubiquitin.
Nitric oxide (NO) is produced by three isoforms of nitric oxide synthase (NOS), which is a chemical messenger that can react with free cysteine residues to form S-nitrothiols (SNOs) . S-nitrosylation is a cell stabilizing protein that regulates gene expression and provides a key PTM for NO donors. The production, localization, activation and catabolism of SNO are strictly regulated.
When one carbon methyl is transferred to nitrogen or oxygen (N- and O-methylation, respectively) to the amino acid side chain, it increases the hydrophobicity of the protein and neutralizes the negative amino acid charge when combined with carboxylic acid. Methylation is mediated by methyltransferase, and S-adenosylmethionine (SAM) is the main methyl donor.
N-acetylation, or the transfer of acetyl groups to nitrogen, occurs in almost all eukaryotic proteins through irreversible and reversible mechanisms.
Lipidation is a method of targeting proteins to organelles (endoplasmic reticulum [ER], Golgi apparatus, mitochondria), vesicles (endosomes, lysosomes) and plasma membranes.
|Depends on the time you need to simulate and the time required for the system to reach equilibrium.
|Product delivery mode
|The simulation results provide you with the raw data and analysis results of molecular dynamics.
CD ComputaBio's post-translational modification service can reduce the cost of subsequent experiments. Post-translational modification service is a personalized and customized innovative scientific research service. Before determining the corresponding analysis plan and price, each project needs to be evaluated. If you want to know more about service prices or technical details, please feel free to contact us. If you want to know more about service prices or technical details, please feel free to contact us.
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