Classical molecular dynamics simulations were performed to investigate the effects of salt on the lower critical solution temperature (LCST) of Poly (N-isopropylacrylamide) (PNIPAM). PNIPAM is often studied as a protein proxy due to the presence of a peptide bond in its monomer unit. PNIPAM is a temperature sensitive polymer which exhibits hydrophobic-hydrophilic phase transition at its LCST. The presence of salt in the solution will shift its LCST, typically to a lower temperature. This LCST shift follows the so-called Hofmeister series. Molecular dynamics (MD) simulations of PNIPAM in 1 M of NaCl, NaBr, NaI, and KCl were carried out to elucidate the effects of different salt on LCST and protein stability. Our results suggest that direct interactions between the salt cations and the polymer play a critical role in the shift of LCST and subsequently on protein stability. Further, cations have a much stronger affinity with the polymer, whereas anions bind weakly with the polymer. Moreover, the cation-polymer binding affinity is inversely correlated with the cation-anion contact pair association constant in solution.