Functional properties of chicken breast meat are affected by heat treatments and the condition of meat, i.e., normal or pale, soft exudative (PSE) meat. The two main fractions of meat proteins, myofibrillar and sarcoplasmic are affected differently by the treatments and the condition of the meat. The aim of this study was to extract myofibrillar and sarcoplasmic proteins from the chicken breast meat and determine differences in protein extractability between normal and PSE meat, and determine temperature transitions in whole muscle and its constituent proteins. The protein concentration of sarcoplasmic protein was less than that of myofibrillar protein in chicken breast muscle. It was also found that the protein solubility differed in normal and PSE muscle. The PSE muscle showed lower protein solubility as compared to the normal muscle which was assumed to be due to the denaturation of some of the protein fractions in PSE muscle. The results of SDS-PAGE did not show much variance in the protein profiles of the PSE and normal samples indicating that the solubilized protein in PSE and normal samples was similar. Thermal denaturation determined using differential Scanning Calorimeter, identified thermal transition peaks which could be of value in the design a scheduled heating sequence for cooking of chicken breast.