Water in the half shell: structure of water, focusing on angular structure and solvation.
Water is a highly polar molecule, consisting of a very electronegative atom, oxygen, bonded to two weakly electropositive hydrogen atoms with two lone pairs of electrons. These features give water remarkable physical properties, some of which are anomalous, such as its lower density in the solid phase compared with the liquid phase. Its ability to serve as both a hydrogen bond donor and hydrogen bond acceptor governs its role as a solvent, a role that is of central interest for biological chemists. In this Account, we focus on water's properties as a solvent. Water dissolves a vast range of solutes with solubilities that range over 10 orders of magnitude. Differences in solubility define the fundamental dichotomy between polar, or hydrophilic, solutes and apolar, or hydrophobic, solutes. This important distinction plays a large part in the structure, stability, and function of biological macromolecules. The strength of hydrogen bonding depends on the H-O...O H-bond angle, and the angular distribution is bimodal. Changes in the width and frequency of infrared spectral lines and in the heat capacity of the solution provide a measure of the changes in the strength and distribution of angles of the hydrogen bonds. Polar solutes and inorganic ions increase the population of bent hydrogen bonds at the expense of the more linear population, while apolar solutes or groups have the opposite effect. We examine how protein denaturants might alter the solvation behavior of water. Urea has very little effect on water's hydrogen bond network, while guanidinium ions promote more linear hydrogen bonds. These results point to fundamental differences in the protein denaturation mechanisms of these molecules. We also suggest a mechanism of action for antifreeze (or thermal hysteresis) proteins: ordering of water around the surface of these proteins prior to freezing appears to interfere with ice formation.
E. R. Johnson Research Foundation and Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Kim A
KA
Sharp
Jane M
JM
Vanderkooi
D019281:Dimerization; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008968:Molecular Conformation; D044367:Phase Transition; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry; D012995:Solubility; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
D011506:Proteins; D014867:Water