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Roles of translational motion of water molecules in sustaining life

Journal

FRONTIERS IN BIOSCIENCE-LANDMARK
Volume 14, Issue -, Pages 3419-+

Publisher

BIOSCIENCE RESEARCH INST-BRI
DOI: 10.2741/3463

Keywords

Water; Life; Entropy; Translational Motion; Self-Assembly; Ordering Process; Protein Folding; Molecular Recognition; Biomolecules; Excluded Volume; Accessible Surface Area; Integral Equation Theory; Liquid State Theory; Molecular Liquids; Morphometric Thermodynamics; Entropic Force; Hydrophobicity; Solvation Thermodynamics; Solvation Free Energy; Partial Molar Volume; Enthalpy-Entropy Compensation; Hydration; Dehydration; Pressure Denaturation; Cold Denaturation; Aggregation; Amyloid Fibril; Alpha-Helix; Beta-Sheet; Side Chains; Native Structure; Conformational Entropy; Hydrogen Bonds; Multipolar Model; Surface Force; Colloidal Suspension; Depletion Potential; Potential Of Mean Force; Lock-Key Interaction; Receptor; Ligand; Dna; B-Z Transition; Actin; Lipid; Biological Membrane; Selectivity; Regularity; Symmetry; Phase Transition; Salt Effect; Isochoric Process; Isobaric Process; Review

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By reviewing the results of our analyses based on statistical-mechanical theories, we point out that the entropic effect arising from the translational motion of water molecules is a principal driving force in a variety of self-assembling and ordering processes in biological systems such as protein folding, molecular recognition, and ordered aggregation of protein molecules. The great entropic loss for the biomolecules accompanying these processes is largely compensated by a great entropic gain of the water that is present in the system. The microscopic mechanisms of protein folding and denaturation, receptor-ligand binding, and amyloid-fibril formation are discussed in detail. We describe an effort to develop a unique method for predicting the native structure of a protein. The roles of NaCl and cosolute molecules are also briefly discussed.

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