The complex hydrogen-bonding arrangement in the biologically important molecule bilirubin IX alpha is probed by using H-1 double-quantum (BQ) magic-angle spinning (MAS) NMR spectroscopy. Employing fast MAS (30 kHz) and a high magnetic field (16.4 T), three law-field resonances corresponding to the different hydrogen-bonding protons are resolved in a H-1 MAS NMR spectrum of bilirubin. These resonances are assigned on the basis of the proton-proton proximities identified from a two-dimensional rotor-synchronized H-1 DQ R;IAS NMR spectrum. An analysis of 1H DQ MAS spinning-sideband patterns for the NK protons in bilirubin allows the quantitative determination of proton-proton distances and the geometry. The validity of this procedure is proven by simulated spectra for a model three-spin system, which show that the shortest distance can be determined to a very high degree of accuracy. The distance between the lactam and pyrrole NH protons in bilirubin is determined to be 0.186 +/- 0.002 nm (corresponding to a dominant dipolar coupling constant of 18.5 +/- 0.5 kHz). The analysis also yields a distance between the lactam NH and carboxylic acid OH protons of 0.230 +/- 0.008 nm (corresponding to a perturbing dipolar coupling constant of 9.9 +/- 1.0 kHz) and an H-H-H angle of 122 +/- 4 degrees. Finally, a comparison of H-1 DQ MAS spinning-sideband patterns for bilirubin and its dimethyl ester reveals a significantly longer distance between the two NH protons in the latter case.