Water compartments in cells.
Human experience in the macrobiological world leads scientists to visualize water compartments in cells analogous to the bladder in the human pelvis or ventricles in the brain. While such water-filled cellular compartments likely exist, the volume contributions are insignificant relative to those of biomolecular hydration compartments. The purpose of this chapter is to identify and categorize the molecular water compartments caused by proteins, the primary macromolecular components of cells. The categorical changes in free energy of water molecules on proteins cause these compartments to play dominant roles in osmoregulation and provide important adjuncts to fundamental understanding of osmosensing and osmosignaling mechanisms. Water compartments possess differences in molecular motion, enthalpy, entropy, freezing point depression, and other properties because of electrostatic interaction of polar water molecules with electric fields generated by covalently bound pairs of opposite charge caused by electronegative oxygen and nitrogen atoms of the protein. Macromolecules, including polypeptides, polynucleotides, and polysaccharides, are stiff molecular chains with restricted folding capacities due to inclusion of rigid ring structures or double amide bonds in the backbone sequence. This creates "irreducible spatial charge separation" between positive and negative partial charges, causing elevated electrostatic energy. In the fully hydrated in vivo state of living cells the high dielectric coefficient of water reduces protein electrostatic free energy by providing polar "water bridge networks" between charges, thereby creating four measurably different compartments of bound water with distinct free energy differences.
Fullerton
Gary D
GD
Department of Radiology, University of Texas HSC at San Antonio, San Antonio, Texas, USA.
Cameron
Ivan L
IL
D002152:Calorimetry, Differential Scanning; D002451:Cell Compartmentation; D003094:Collagen / Q000737:chemistry; D004798:Enzymes / Q000378:metabolism; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular; D009995:Osmosis / Q000502:physiology; D009997:Osmotic Pressure; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D014867:Water / Q000737:chemistry / Q000502:physiology*
D004798:Enzymes; D011506:Proteins; D014867:Water; D003094:Collagen