We review the results of compressibility studies on proteins, nucleic
acids, and systematically altered low molecular weight compounds that
model the constituents of these biopolymers. The model compound data a
llow one to define the compressibility properties of water surrounding
charged, polar, and nonpolar groups. These results, in conjunction wi
th compressibility data on proteins and nucleic acids, were used to de
fine the properties of water that is perturbed by the presence of thes
e biopolymers in aqueous solutions. Throughout this review, we emphasi
ze the importance of compressibility data for characterizing the hydra
tion properties of solutes (particularly, proteins, nucleic acids, and
their constituents), while describing how such data can be interprete
d to gain insight into role that hydration can play in modulating the
stability of and recognition between biologically important compounds.