This　study　investigated　the　cryoprotective　mechanism　of　ultrafiltration　membrane-separated　fractions　(＞10　kDa,　UF-1;　3-10　kDa,　UF-2;　and　＜3　kDa,　UF-3)　derived　from　silver　carp　hydrolysates　on　frozen　surimi.　The　surimi　gel　incorporating　UF-3　exhibited　a　compact,　continuous　structure　with　uniform　pores,　even　after　undergoing　six　freeze-thaw　(F-T)　cycle,　with　the　minimal　reduction　in　entrapped　water　(from　95.1　%　to　91.1　%)　and　least　increase　in　free　water　(from　4.5　%　to　6.6　%)　as　revealed　by　SEM　and　LF-NMR　analysis.　Through　molecular　docking　analysis,　three　major　peptides　in　UF-3　were　identified　to　form　robust　interactions　with　the　myosin　head　pocket,　facilitated　by　hydrogen　bonds,　electrostatic　forces,　and　hydrophobic　interactions.　Furthermore,　molecular　dynamics　simulations　demonstrated　that　the　three　peptides　effectively　prevented　myosin　from　unfolding　and　aggregating　by　tightly　binding　to　basic　amino　acids　(Arg,　Lys)　and　hydrophobic　amino　acids　(Phe,　Leu,　Ile,　Met,　and　Val)　residues　in　the　myosin　head　pocket,　primarily　governed　by　electrostatic　energies　(-156.95,　-321.38,　and　-267.53　kcal/mol,　respectively)　and　van　der　Waals　energies　(-395.05,　-347.46,　and　-319.16　kcal/mol,　respectively).　Notably,　the　key　action　site　was　identified　as　Lys599　on　myosin.　The　hydrophilic　and　hydrophobic　hotspot　residues　of　the　peptides　worked　synergistically　to　stabilize　the　myosin　structure　in　frozen　surimi.