Analysis of our Plasmodium falciparum malaria parasite peptides' H-1-NMR database in the search for H-bonds and pi-interactions led us to correlate their presence or absence with a peptide's particular immunological behavior. It was concluded that a 26.5 +/- 1.5 angstrom between positions 1 to 9 of the HLA-DR beta 1(x) interacting region was necessary for proper docking of 20mer-long peptides and these MHC Class II molecules for full-protective immunity. Presence of intramolecular H-bonds or pi-interactions leading to righ-handed alpha-helix or beta-turn conformation in this peptide's region induces different immune responses or none. PPIIL conformation and the absence of any intramolecular interaction thus became the first feature characterising our immune protection-inducing structures as malaria vaccine candidates. (C) 2017 Elsevier Inc. All rights reserved.