A new modification of pulsed-ionization high-pressure mass spectrometry (PHPMS) has been used to perform equilibrium thermochemical studies for relatively nonvolatile biomolecules such as amino acids. Binding enthalpy and entropy changes have been measured for proton-bound clusters of glycine, which are in good agreement with both theoretical (DFT) results of this work and a previous blackbody infrared dissociation experiment. Experimental data indicate that a number of conformers of the proton-bound dimer of glycine may coexist in the explored temperature range (360-460 K). Several new, conceptually different isomers (two of them zwitterionic) have been found by DFT calculations, one of which is 7 kJ mol(-1) lower in energy than the structure previously reported to be the energy minimum.