Abstract: This study was conducted to investigate the effect of salt on the quality and myofibrillar protein during cold storage of chicken breast. After the low-temperature curing with different salt concentration (0.0%, 1.6%, 3.2%, 4.8%, 6.4% and 8.0%) for different times (0.2, 1, 2, 3, 4 d), the chicken samples were used to meaure the water content, water holding capacity, olubility, surface hydrophobicity, carbonyl content, sulfhydryl content, and dimer tyrosine content. Results showed that water holding capacity and surface hydrophobicity were changed after brining, the brining time positively affected carbonyl content and dimer tyrosine content while negatively affected sulfhydryl group content, thermal stability, and solubility. In addition, salt treatments could change the structure of samples from α-helix to β-fold. With the increasing of salt concentration, the contents of carbonyl and dimer tyrosine increased firstly and then decreased, and the content of sulfhydryl increased continuously. When the salt concentrations ranged from 3.2% to 4.8%, the characteristic indexes of myofibrillar protein changed obviously. In conclusion, the structure and function of myofibrillar protein in chicken were affected by salination. These results would provide theoretical data for controlling the changes of chicken quality and oxidation of myofibrillar protein during the brining process.