Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 15, 307-319

Protein Post-Translational Modifications: In silico Prediction Tools and Molecular Modeling


Protein Post-Translational Modifications: In silico Prediction Tools and Molecular Modeling

Martina Audagnotto et al. Comput Struct Biotechnol J.


Post-translational modifications (PTMs) occur in almost all proteins and play an important role in numerous biological processes by significantly affecting proteins' structure and dynamics. Several computational approaches have been developed to study PTMs (e.g., phosphorylation, sumoylation or palmitoylation) showing the importance of these techniques in predicting modified sites that can be further investigated with experimental approaches. In this review, we summarize some of the available online platforms and their contribution in the study of PTMs. Moreover, we discuss the emerging capabilities of molecular modeling and simulation that are able to complement these bioinformatics methods, providing deeper molecular insights into the biological function of post-translational modified proteins.


Fig. 1.
Fig. 1
Schematic representation of PTMs discussed in this review.

Similar articles

See all similar articles

Cited by 21 PubMed Central articles

See all "Cited by" articles


    1. Walsh C. Roberts and Company Publishers; 2006. Posttranslational modification of proteins: Expanding nature's inventory.
    1. Walsh C.T. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed. 2005;44:7342–7372. - PubMed
    1. Rocks O. An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science. 2005;307:1746–1752. - PubMed
    1. Fairbank M. RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase. FEBS Lett. 2012;586:2488–2493. - PubMed
    1. Maeda A. Palmitoylation stabilizes unliganded rod opsin. Proc Natl Acad Sci. 2010;107:8428–8433. - PMC - PubMed

LinkOut - more resources