We describe a method for determining the torsion angle phi in peptides. The technique is based on the measurement of the relative orientation of the N-H-N and C-alpha-H-alpha bonds, which is manifested in the rotational sideband spectrum of the sum and difference of the two corresponding dipolar couplings. The method exploits N-15-C-13 double-quantum and zero-quantum coherences, which evolve simultaneously under the N-H and C-H dipolar interactions. The magnitudes of these dipolar couplings scaled by the proton homonuclear decoupling sequence are directly extracted from control experiments that correlate the dipolar interactions with the isotropic chemical shifts. Applied to N-15-labeled N-acetyl-D,L-valine, the experiment yielded phi = -135 degrees, which agrees well with the X-ray crystal structure. Simulations indicate that the accuracy of the measured angle phi is within +/-10 degrees when the N-H-N and C-alpha-H-alpha bonds are approximately antiparallel and +/-20 degrees when they are roughly parallel. The technique is sufficiently sensitive to be applied to small peptides that are only labeled in N-15 and to larger polypeptides that are uniformly and randomly labeled in both N-15 and C-13. It allows phi angles in various residues to be measured simultaneously and resolved by the C-alpha chemical shifts.