Many peptides, proteins, natural compounds and drugs bind to biological membranes. Determining their topology is crucial in understanding their function and activity on a molecular level. Here new solution state NMR methods for obtaining the complete orientation and location of helical peptides in a membrane-mimetic environment (micelle-bound) are presented. By monitoring proton T1 - relaxation rates during a titration with a paramagnetic surface probe, a wave-like pattern with a periodicity of 3.6 residues per turn was obtained. The water-soluble paramagnetic agent Gd(DTPA-BMA) was used due to its reported absence of interactions with proteins. The relaxation rates at different concentrations of the paramagnetic compound were derived from the cross-peaks of saturation-recovery 2D-NOESY and 2D-TOCSY spectra on the antimicrobial fifteen residues peptide CM15 and the twenty five residues peptide TM7 that mimics the Vph1p transmembrane helix 7 of yeast V-ATPase, both in unlabeled form. The obtained wave-like pattern, the paramagnetic relaxation wave, allows the determination of the rotation (azimuth) and tilt angle of the helix. The location of the peptides in terms of their immersion depths was obtained based on the ParaPos approach. The measured paramagnetic relaxation enhancements (PREs) of protons were correlated with their micellar immersion depths after calibration using a system of known topology, in this case a transmembrane helical peptide TM7. The orientation and immersion depth of the TM7 and CM15 peptides were then obtained by least-square fitting of measured versus calculated PREs.The presented methods enable the complete orientation and location of the peptide in the micelle to be obtained even on unlabeled peptides by one simple experiment that does not require any covalent modifications of the peptide. The approaches also open a path towards the topology determination of any structurally characterized micelle bound molecule.