PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides

By Pierre Thévenet, Yimin Shen, Julien Maupetit, Frédéric Guyon, Philippe Derreumaux, Pierre Tufféry. Nucleic Acids Res., 2012

632 citations recorded by the source corpus.

In the context of the renewed interest of peptides as therapeutics, it is important to have an on-line resource for 3D structure prediction of peptides with well-defined structures in aqueous solution. We present an updated version of PEP-FOLD allowing the treatment of both linear and disulphide bonded cyclic peptides with 9–36 amino acids. The server makes possible to define disulphide bonds and any residue–residue proximity under the guidance of the biologists. Using a benchmark of 34 cyclic peptides with one, two and three disulphide bonds, the best PEP-FOLD models deviate by an average RMS of 2.75 Å from the full NMR structures. Using a benchmark of 37 linear peptides, PEP-FOLD locates lowest-energy conformations deviating by 3 Å RMS from the NMR rigid cores. The evolution of PEP-FOLD comes as a new on-line service to supersede the previous server. The server is available at: http://bioserv.rpbs.univ-paris-diderot.fr/PEP-FOLD.

Subfields: Microbiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/6fa25c6831859b883dd761790e56a8ca475635a7

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In Molecular Biology

1. Pierre Thévenet
2. Julien Rey
3. Alexis Lamiable
4. Marek Vavrusa
5. Philippe Derreumaux
6. Pierre Tufféry

Citations in the corpus

• PEP-FOLD3: faster de novo structure prediction for linear peptides in solution and in complex (2016, methodology): “These include facilities such as CycloPS (11) for the preparation of cyclic peptides, and servers for the de novo structure prediction of peptides, including PEPStr and PEPStrMod (12), PEP-FOLD (13,14) and PEPLook (15).”