Infrared reflection-absorption spectroscopy (IRRAS) intensities of the Amide I vibration are used to develop a quantitative approach for determining the Euler angles that describe the orientation of protein beta-sheets in aqueous monolayer films. A synthetic amphipathic peptide, Val-Glu-Val-Orn-Val-Glu-Val-Orn-Val-Glu-Val-Orn-Val-OH is used as a test case. The pattern of Amide I frequencies suggests that the molecule is organized as an antiparallel beta-sheet at the air/water interface. The model used to simulate the Amide I intensities reveals that the beta-sheet has a slight preferential alignment parallel to the direction of compression; i.e., deviation from uniaxial symmetry is observed. In addition, the sheet is found to lie flat on the aqueous surface, with (presumably) the polar side chains interacting with the aqueous subphase. Limitations and advantages of the theoretical approach are discussed.