As amazing as it may seem, the spatial structures of the molecules of life may mimic the order/disorder properties of the environment in which they evolved.
Some regions on their surfaces hydrogen bond with surface water in the same dynamic manner that liquid water molecules bond with each other, while other regions induce surface water to form lower-energy ice-like units of cubic hydration order. As polypeptides are released from ribosomes, it is primarily the lipid regions which, by initially-forming ice-like elements on their surfaces and then losing that unstable water, assemble together spontaneously to produce the anhydrous cores of proteins. Transient linear elements of hydration which then form between ordering and ionic centers on surfaces of molecules as they approach each other, lead them into functional associations which. sometimes, mimic the cubic spatial units which formed them, sometimes alternate symmetry units and, sometimes, spherical units, like those of water molecules around isolated ions. Cells are amazing worlds of order and disorder. Have fun reading
The Order/Disorder properties of water appear to play a critical role in the catalytic hydrolyses of aromatic peptides from the ends of polypeptide chains. Here is a graphic interpretation of that role.
Ribonuclease A is presented below as an example of how surface water, by repetitively forming picosecond ice-like linear elements of hydration on lipid surfaces of its polypeptide, not only directs and drives its wrapping and assembly into its unique protein structure, but its enzymatic activity as well.