Post-translational modification (PTM) refers to the covalent modification and general enzymatic modification of proteins during or after biosynthesis in cells. To date, more than 350 different PTMs have been experimentally discovered in vivo, indicating their important role in regulating cellular processes. PTM mainly appears in the amino acid side chain or the N or C terminal of the protein. They play a key role in expanding the diversity of protein activity by introducing new functional groups (such as phosphate, acetate, amide or methyl), leading to changes in enzyme activity, ligand affinity, protein-protein interactions, and protein stability. Structural changes may also occur at the main chain level, especially in the formation of disulfide bonds and proteolytic cleavage of proteins at peptide bonds.
In recent years, high-throughput experimental methods based on mass spectrometry have been developed and are gaining popularity.
In addition, PTM computational modeling represents another attractive method with its accuracy, speed and convenience.
ComputaBio uses computational modeling to predict potential PTM sites in proteins, and to model side-chain and main-chain conformations to reflect changes caused by common PTMs.
Our algorithms are trained using existing PTMs observed in the Protein Data Bank and proven to be fast and accurate.
Figure 1. Computational modeling of post-translational modifications.
|Project name||Post-translational modification services|
|Samples requirements||Our Post-translational modification services require you to provide specific requirements.|
|Detection cycle||Decide according to your needs.|
|Service including||We provide you with raw data and modeling results.|
|Acetylation||Usually add acetyl to the N-terminus of the protein.|
|Alkylation||Add alkyl such as methyl or ethyl.|
|Methylation||A common type of alkylation, adding methyl groups to the side chain amino groups of lysine, arginine, etc.|
|Glutamate||Establish a covalent bond between glutamic acid and cathelicidin and other proteins.|
|Glycine||A covalent bond is established between the C-terminus of catechin and one to more than 40 glycines.|
|Isoprene||Add isoprene such as farnesol and tetraisoprene.|
|Sulfation||Add sulfate to tyrosine to amidate the selenized C-terminal.|
Our Post-translational modification services have proven to be very useful for understanding the biochemical basis of physiological events at different stages of drug development (even in different fields such as materials science). Our team of experts can provide accurate modeling and analysis on the system of interest. ComputaBio team has been working in this field for more than ten years and has published his findings in top scientific journals. If you have a need for protein structure modeling services, please feel free to contact us.
We provide a variety of modeling services, but not limited to: