The homodimeric representative of the applied peptide motif H-(Tyr-Tyr) 4 -Lys-OH has already been shown to enable intermolecular interaction via its phenolic sidechain pattern within the aqueous phase (Alexopoulos et al. 2004 ). The homodimer species 2 adopts a membrane spanning orientation in DLPC bilayers (Küsel et al. 2007) and likewise tends to aggregation (Schneggenburger et al. 2009 ). Therefore, the GID approach was undertaken to evaluate if the latter observation of a membrane insertion and transmembrane alignment is likewise true for the designed hairpin species (2) and the recognition system (3) (Fig. 2) . Furthermore, it was our aim to screen the samples for any evidence of lateral peptide interaction, i.e., the formation of higher-order structures (low q k , q z ), as sometimes indicated by superstructure peaks (Constantin et al. 2007 ) as well as for regular intrahelical distances that can be revealed from the occurence of so-called helix peaks (Spaar et al. 2004 ).