An analysis based on an extension of Zwanzig's model of protein folding indicates that global downhill folding proteins should reveal different apparent melting temperatures (Tms) when monitored by different techniques. This was experimentally confirmed in the protein BBL mentioned above. The unfolding followed by differential scanning calorimetry (DSC), circular dichroism (CD), fluorescence resonance energy transfer (FRET) and fluorescence all revealed different apparent melting temperatures. A wavelength-dependent melting temperature was also observed in the CD experiments. The data analyzed with a structure-based statistical mechanical model resulted in a unimodal population distribution at all temperatures, indicating a structurally uncoupled continuous unfolding process. The crucial issue in such experiments is to use probes that monitor different aspects of the structure. For example, DSC gives information on the heat capacity changes (and hence enthalpy) associated with unfolding, fluorescence on the immediate environment of the fluorophore, FRET on the average dimensions of the molecule and CD on the secondary structure.