This study investigated the effects of different pH conditions on the function of myofibrillar protein in rabbit meat, the correlation between the functional indexes of myofibrillar protein and the mechanism of protein tertiary structure. It was found that, with the pH approaching the isoelectric point range, the aromatic amino acids inside the protein were exposed, the tertiary structure of the protein was unfolded, and the surface hydrophobicity became larger, which resulted in the increase of the hydrophobic interaction between the proteins. Changes in myofibrillar protein structure cause protein solubility to decrease, and accompanied by decreased emulsifying activity and changes in emulsion stability. At the same time, this structural change leads to the change of myofibrillar protein rheological properties. The decrease of pH leads to the decrease of shear stress, and the shear stress changes obviously at the near isoelectric point. With the decrease of pH, the hardness of myogenic protein gel increases, and becomes smaller at near isoelectric point. At the same time, the gel retention of gel is decreasing and the gel whiteness is increasing.