I agree with Adam B Shapiro . Guanadinium hydrogenchloride on its own has pKa closer to 12, and is therefore going to have no buffering capacity at pH 7.4.
If I understand you rightly, Vijay, you are saying that the protein did not unfold when you buffered everything at pH 7.4? i.e. both the protein and the GdHCl were buffered... If that is so, then you didn't get a bad result at all, but rather a very good one. It indicates that any previous unfolding you were seeing was a pH effect rather than a GdHCl effect. This alters how you judge the relative stability of this protein to your standard and other proteins, but at least it is a clear result. The protein is more stable than you think.
Unless you aren't saying the protein didn't unfold or that you had everything buffered. Then it would just be a completely unclear result.