Welcome to PEPstrMOD

The PEPstrMOD server predicts the tertiary structure of small peptides with sequence length varying between 7 to 25 residues. It also handles peptides having various modifications like non-natural residues, terminal modifications (Acetylation/Amidation), Cyclization (N-C, disulfide bridges), conversion of L- to D- amino acids, post translational modifications, etc. The prediction strategy is based on the realization that β-turn is an important and consistent feature of small peptides in addition to regular structures. Thus, the method uses both the regular secondary structure information predicted from PSIPRED and β-turns information predicted from BetaTurns. The structure is further refined with energy minimization and molecular dynamic simulations.

If you are using PEPstrMOD, please cite the following articles:
i) Singh, S., Singh, H., Tuknait, A., Chaudhary, K., Singh, B., Kumaran, S. and Raghava, G.P.S. (2015) PEPstrMOD: structure prediction of peptides containing natural, non-natural and modified residues. Biology Direct 10:73.
ii) Kaur, H., Garg, A. and Raghava, G.P.S. (2007) PEPstr: A de novo method for tertiary structure prediction of small bioactive peptides. Protein Pept Lett. 14:626-30.
Click Here for PEPstrMOD Manual