The variation of water cluster structure of Zn（NO3）2 dilute aqueous solution before/after frozen/thawed disposition and its effect on the conformation of bovine serum albumin（BSA） were studied in this paper.The conductivity，density and viscosity of Zn（NO3）2 dilute aqueous solution before/after frozen/thawed disposition were determined to show the variation of water cluster structure of Zn（NO3）2 dilute aqueous solution，which indicated that the freezing/thawing disposition on Zn（NO3）2 dilute aqueous solution resulted in the obvious increase of conductivity and viscosity，and decrease of density，because of the forming of smaller water cluster structure binded by hydrogen bond in Zn（NO3）2 dilute aqueous solution after frozen/thawed disposition.The conformation of BSA interacted with Zn（NO3）2 dilute aqueous solution before/after frozen/thawed disposition was studied by laser confocal Raman microspectroscopy，Fourier transform infrared（FTIR） spectroscopy and circular dichroism（CD） spectrum.The result indicated that Zn2+ ions affect the amideⅠbands of BSA，causing the decrease of the α-helices in BSA.The configuration of disulfide bonds and the microenvironment of tyrosine and tryptophan changed owing to the effect of Zn2+ ions on BSA.The freezing/thawing disposition on Zn（NO3）2 dilute queous solution decreased the effect on the conformation of BSA，which caused less decrease of α-helices in BSA amideⅠbands，and weakened the effect on the microenvironment of tyrosine.It can be concluded that the freezeing/thawing disposition on Zn（NO3）2 dilute aqueous solution can change the water cluster structure of the dilute aqueous solution，resulting in the change of the physicochemical property of Zn（NO3）2 dilute aqueous solution，and then weakened its effect on the conformation of BSA.