The identification of physicochemical parameters controlling binding interactions between food components and flavour compounds in model system is predominant to understand flavour perception (Guichard, 2002). In this way, molecular interaction processes were investigated in a simple food model composing of a whey protein, the β-lactoglobulin (β-LG) in its monomeric form, and aroma compounds by two spectroscopic techniques. Nuclear Magnetic Resonance (NMR) combined with Fourier Transform Infrared (FTIR) give information on the binding site location and structural changes of the protein respectively. Relations between these experimental results and the molecular properties of flavour compounds were investigated to obtain predictive models by Quantitative Structure-Activity Relationships (QSAR)modelisation approach(Tromelin and Guichard, 2004). General results confirmed the existence of at least two different binding sites for aroma compounds on β-LG. According to its structure, flavour compounds seem to interact with the central cavity or with an external site located in a groove between the outer side-chains of the β-barrel and the α-helix.