Water and Biological MacromoleculesWesthof Water and Biological Macromolecules presents an excellent description of the structural aspects of water molecules around biological macromolecules. Topics discussed include the properties of water in solid and liquid states; proteins, nucleic acids, polysaccharides, and lipids; and theoretical approaches for understanding the macroscopic observations and integrating microscopic descriptions. The nature and roles of hydration forces in macromolecular complexation and cell-cell interactions are explained, in addition to phenomena such as entropy-enthalpy compensation and the thermodynamic treatment of water bridging. Water and Biological Macromolecules will be a valuable reference for biophysicists, biochemists, and macromolecular biologists. |
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Page 160
... backbone polar atoms hydrogen bonded to water molecules . ( b ) The backbone NH and CO groups form hydrogen bonds within the chain and the water molecules are eliminated . These two modes of backbone hydration are ubiquitous in protein ...
... backbone polar atoms hydrogen bonded to water molecules . ( b ) The backbone NH and CO groups form hydrogen bonds within the chain and the water molecules are eliminated . These two modes of backbone hydration are ubiquitous in protein ...
Page 440
Westhof. Figure 14.2 A schematic presentation of the ' backbone ' of a globular protein and a few side - chains protruding from the ' backbone ' . The term ' backbone ' refers here to that part of the protein which is included in the ...
Westhof. Figure 14.2 A schematic presentation of the ' backbone ' of a globular protein and a few side - chains protruding from the ' backbone ' . The term ' backbone ' refers here to that part of the protein which is included in the ...
Page 443
... backbone . One cannot assume that the backbone will cause a uniform shift in the values of the solvation Gibbs energies of the side - chains . Different side - chains are expected to be affected differently by the presence of the ...
... backbone . One cannot assume that the backbone will cause a uniform shift in the values of the solvation Gibbs energies of the side - chains . Different side - chains are expected to be affected differently by the presence of the ...
Contents
Water structure | 3 |
Thermodynamic and dynamic properties of water | 45 |
Aqueous solutions of simple hydrophobic solutes | 55 |
Copyright | |
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Common terms and phrases
Acta Cryst analysis anionic aqueous atoms B-DNA B-form backbone base pairs Beveridge binding Biochemistry Biochim Biol Biomol Biophys Biopolymers calculations Cevc chain Chem Clementi complex conformation counterions crystal structure crystalline crystallographic d(CGCGAATTCGCG density distance dodecamer electron electrostatic Equation experimental Figure force field free energy function Gibbs energy Goodfellow H-bond helix hydration hydration forces hydration shell hydrogen bonds hydrophilic hydrophobic ice Ih interactions interfacial ions lipid bilayers lipid headgroups liquid macromolecules MD simulation membrane minor groove mJ/m² molecular dynamics Molecular dynamics simulation Monte Carlo neutron diffraction nucleic acids nucleotide orientation oxygen phase phosphate groups phosphatidylcholine phospholipid Phys polar polymer polysaccharides potential refinement region relaxation repulsive residues resolution Saenger side-chains solution solvation solvation Gibbs energy solvent solvent molecules solvent structure ẞ-sheet stability Struct studies surface temperature tion water bridges water molecules water structure Westhof X-ray Z-DNA