There is significant interest in solving high-resolution dynamic structures of membrane-associated peptides using solid-state NMR spectroscopy. Previous solid-state NMR studies have provided valuable insights into the functional properties of an exciting class of biomacromolecules such as antimicrobial peptides and amyloid peptides. However, it has been a major challenge to apply solid-state NMR techniques to study peptides or proteins that are not labeled with specific isotopes such as C-13, N-15, and/or H-2. This study utilizes 2D H-1/H-1 radio frequency-driven recoupling (RFDR) and nuclear Overhauser effect spectroscopy (NOESY) pulse sequences under magic angle spinning to study a membrane-bound antimicrobial peptide MSI-78 (or also known as pexiganan). We demonstrate that proton resonances can be assigned and structural constraints, NOE and H-1-H-1 dipolar couplings, can be measured without the need for any isotopic enrichment. The buildup curves, showing the dependence of the cross peak intensity against the mixing time, obtained from 2D H-1/H-1 NOESY and RFDR experiments are compared. Our results reveal that the RFDR-recovered H-1/H-1 dipolar couplings associated with alpha and side chain protons are larger than that with the amide-protons. This study provides a means to measure residual H-1/H-1 dipolar couplings for the investigation of structure, dynamics, and aggregation of peptides using a suitable model membrane like micelles or bicelles.