The seminal contributions of Ulrich Haeberlen to homonuclear line narrowing and the determination of1H chemical shift tensors are crucial for protein structure determination by solid-state nuclear magnetic resonance spectroscopy. The1H chemical shift is particularly important in spectra obtained on oriented samples of membrane proteins as a mechanism for providing dispersion among resonances that are not resolved with the1H-15N dipolar coupling and15N chemical shift frequencies. This is demonstrated with three-dimensional experiments on uniformly15N-labeled samples of Magainin antibiotic peptide and the protein Vpu from HIV-1 in oriented lipid bilayers. These experiments enable resonances in two-dimensional1H-15N dipolar coupling/15N chemical shift planes separated by1H chemical shift frequencies to be resolved and analyzed. These three-dimensional spectra are compared to one-dimensional spectra of full-length Vpu, the cytoplasmic domain of Vpu, and Magainin, as well as to two-dimensional spectra of fd coat protein and Colicin El polypeptide. The1H amide chemical shift tensor provides valuable structural information, and this is demonstrated with its contributions to orientational restrictions to one of the in-plane helical residues of Magainin.