Abstract We use resonance Raman spectroscopy to study cytochrome c, hemoglobin and myoglobin from 50 μM solutions dried on a SiO 2 surface. Intense Raman spectra were observed with low luminescent background when excited at 488 nm with low laser power levels (0.6 mW) and relative short acquisition times (120 s). We estimate that 1 picogram of heme proteins can be detected. A polarization sensitive Raman band in cytochrome c near the edge of dried droplets suggests that the proteins line up in the ring deposit. This preferential orientation is suggested to contribute to the low luminescence back ground signal and to the larger Raman intensity compared to the heme proteins in powder form.