Post-translational Modification Service

Computational modeling of post-translational modifications

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.

Overall Solution

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.

CD 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.

Computational modeling of post-translational modifications. Figure 1. Computational modeling of post-translational modifications.

Our Post-translational Modification Services

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.
Price Inquiry

Service details

Reactions Descriptions
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.


  • PTM site prediction based on sequence and structure.
  • An accurate model for simulating residues.
  • Manipulating PTMs that involve changes to the main chain.
  • Refinement of energy-based modified protein structure.
  • Include ligands, cofactors and water in the model.
  • Predict physical properties and compare with unmodified proteins.

Post-translational Modification Service 2

Our Advantages

  • CD ComputaBio can perform conformation modeling on both side chain and main chain.
  • The protein constructed by CD ComputaBio can reflect changes caused by post-translational modifications.
  • CD ComputaBio' post-translation modification service has proven to be accurate and fast in multiple projects.

Post-translational Modification Service 3

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. CD 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:

* It should be noted that our service is only used for research, not for clinical use.


  • Verification code


© 2021 CD ComputaBio. All rights reserved.