Fluorescence spectroscopy is an established technique for monitoring protein unfolding events induced through variations in temperature, pH, or chaotropic agent. In certain circumstances, a protein's intrinsic tryptophan fluorescence can provide insight into changes in tertiary structure precluding the need for an external chromophore.  Changes in native fluorescence are recorded and analysed by plotting the wavelength maxima and fluorescence intensity against variation in denaturant. Different reduction procedures can be applied to this primary data to determine characteristic points relating to the protein denaturation profile. Although all methods of primary analysis yield a sigmoidal-like function there is often a disparity in characteristic parameters (such as melting temperature) extracted when using different analytical approaches. In this poster, we propose a novel method of primary analysis which involves measuring the peak-to-peak distance between fluorescence spectra of a protein induced to unfold through temperature ramping. We compare our novel approach to existing methods by applying them to the native tryptophan fluorescence spectra of several model proteins subjected to thermal unfolding.