The technique of frozen matrix-assisted laser ablation coupled with resonance-enhanced multiphoton ionization and reflectron time-of-flight mass spectrometry was used to detect intact organic molecules directly from solutions. When frozen at the temperature of liquid nitrogen, the matrices of interest were ablated by a pulsed C 0 2 single-mode laser. The analyte molecules emerging from the ablated plume were then ionized by a tunable XeCl excimer laser-pumped dye laser and analysed with a gridless reflectron time-of-flight mass spectrometer. The ablation process from an ice matrix was studied with the amino acids tryptophan and tyrosine dissolved in an aqueous ethanol solution to a concentration level of 5 X M. It was found that fragmentation of the analyte molecules is strongly dependent on the ablating laser fluence and that there is a laser fluence range just above the ablation threshold where the decomposition is negligible. The different fragmentation mechanisms are discussed and a cavitation under the liquid surface, causing the sonoluminescence signal from an ice matrix, was shown to be responsible for the decomposition of the analyte molecules ablated by a low photon energy IR laser. Under the appropriate conditions, the analyte molecules were found to have a low rotational temperature of about 150 K resulting from the jet-like cooling in multiple collisions with matrix molecules.