To improve the gel quality of pale, soft, and exudative (PSE)-like chicken protein isolate (PPI) obtained via ultrasound-assisted alkaline extraction (UAE), l-lysine (l-Lys), l-arginine (l-Arg), or l-histidine (l-His) were used and the effects on the thermal gelling characteristics of PPI were studied. Compared with the nonbasic amino acid addition group, the addition of l-His/l-Arg/l-Lys significantly increased the solubility and absolute zeta potential of PPI, whereas reduced the particle size and turbidity (p < 0.05). They enhanced the gel strength and textural properties of PPI (p < 0.05) and reduced the cooking loss of PPI in the following order: l-Lys > l-Arg > l-His. The solubility, gel strength, and hardness of PPI with l-Lys were increased by 18.6%, 44.6%, and 57.6%, respectively, and cooking loss was decreased by 18.1%. Low-field nuclear magnetic resonance and magnetic resonance imaging revealed that basic amino acids addition decreased the water mobility in PPI gels with increasing immobile water content. Scanning electron microscopy revealed that the addition of basic amino acids promoted the formation of a more uniform and tight network microstructure in PPI gels. The α-helix content was decreased, whereas the β-sheet content was increased in PPI gels after basic amino acid addition. Therefore, addition of basic amino acids, especially l-Lys, enhances the gel properties of PPI. PRACTICAL APPLICATION: This study revealed that adding basic amino acids effectively improved the gel properties of PPI obtained via UAE method, with l-Lys exerting the best improvement effect. Our findings highlight the application value of PSE-like meat by the improvement of gel characteristics of PPI, providing a theoretical reference for the processing and utilization of PPI.