@article {2016|1733,
	title = {PEP-FOLD3: faster denovo structure prediction for linear peptides in solution and in complex},
	journal = {Nucleic Acids Res.},
	volume = {44},
	number = {W1},
	year = {2016},
	pages = {W449-W454},
	abstract = {Structure determination of linear peptides of 5-50 amino acids in aqueous solution and interacting with proteins is a key aspect in structural biology. PEP-FOLD3 is a novel computational framework, that allows both (i) de novo free or biased prediction for linear peptides between 5 and 50 amino acids, and (ii) the generation of native-like conformations of peptides interacting with a protein when the interaction site is known in advance. PEP-FOLD3 is fast, and usually returns solutions in a few minutes. Testing PEP-FOLD3 on 56 peptides in aqueous solution led to experimental-like conformations for 80\% of the targets. Using a benchmark of 61 peptide-protein targets starting from the unbound form of the protein receptor, PEP-FOLD3 was able to generate peptide poses deviating on average by 3.3 angstrom from the experimental conformation and return a native-like pose in the first 10 clusters for 52\% of the targets. PEP-FOLD3 is available at http://bioserv.rpbs.univ-paris-diderot.fr/services/PEP-FOLD3.},
	issn = {0305-1048},
	doi = {10.1093/nar/gkw329},
	author = {Lamiable, Alexis and Thevenet, Pierre and Rey, Julien and Vavrusa, Marek and Philippe Derreumaux and Pierre Tuffery}
}
@article {2012|1944,
	title = {PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides},
	journal = {Nucleic Acids Res.},
	volume = {40},
	number = {W1},
	year = {2012},
	month = {jul},
	pages = {W288-W293},
	doi = {10.1093/nar/gks419},
	author = {Thevenet, Pierre and Shen, Yimin and Maupetit, Julien and Guyon, Frederic and Philippe Derreumaux and Pierre Tuffery}
}
