Recent experiments and numerical simulations have shown that the water molecules confined on the surfaces of some substrates, including the surfaces of cellular components in tissues and cells, form icelike ordered structures. If a protein folds in an environment with those icelike ordered water molecules, its behavior may be different from that in bulk water. Here, the effect of this ordered water environment on protein folding is studied by using an off-lattice Gō-like model. It is found that the ordered water environment significantly improves the native state stability and greatly speeds up the folding rate of the proteins.