The impact of temperature and charge on the conformation of tryptamine (Tryp) is examined in the gas phase by infrared laser-vibrational predissociation spectroscopy in the 2800-3800 cm(-1) region. Previous studies of neutral Tryp(H(2)O)(n) clusters showed preferential stabilization of specific tryptamine conformers through hydrogen bonding. When complexed with the biologically significant potassium ion, the only conformers found to form under these experimental conditions are built on hitherto unobserved neutral Tryp conformers. The electrostatic interaction between K(+), the tryptamine NH(2) lone pair, and the indole ring in K(+)(Tryp) favors the formation of these new conformers. The observed K(+)(Tryp)(H(2)O) conformers vary significantly from the previously reported neutral Tryp(H(2)O) structure. Using the argon tagging method, we show how variations in temperature impact the observed infrared spectra, demonstrating that different conformers are populated under the different experimental conditions. In addition, the presence of a high-energy conformer of K(+)(Tryp)(H(2)O), trapped by the argon evaporative cooling process, was identified. Exploring the conformational landscape of hydrated cluster ions bearing flexible biomolecules is now possible.