Instead, we observed that PEGylation slows solvent dynamics surrounding the surface of Gal3C, with the magnitude of this effect correlating with the length of the conjugated polymer. PEGylation-driven slowing of solvent dynamics correlated with the formation of a shroud-like protein-PEG conformation and with the increased thermal stability and redirection of the Gal3C unfolding pathway. By integrating experimental and computational approaches across multiple timescales, 2D IR and MD simulations for fast solvent dynamics, and NMR spectroscopy for slower protein-polymer interactions, we not only validate the accuracy of the simulations but also reveal a mechanistic link between polymer length and conjugate stability. Our findings suggest that a minimum polymer length is required to sufficiently slow proteinsolvent dynamics and enhance stability, providing criteria for the intentional design of stabilized conjugates.