Proteins are known to undergo denaturation and form different phases with varying physicochemical parameters. We report unusual stability of bovine serum albumin protein against commonly used denaturants (temperature and surfactant) in  the charged reversal reentrant phase, caused by the multivalent counterions. Unlike monovalent counterions, which promote the denaturants’ induced protein unfolding, the unfolding is restricted in the presence of multivalent ions. The observations are beyond the scope of general understanding of protein unfolding and are believed to be governed by ion-ion correlations driven strong condensation of the multivalent ions.