Physical Review Letters · 2010 · 52 citations · 13 references
Natural SciencesBiochemistryBiophysicsBiophysical ChemistryMolecular BiophysicsNucleic Acid BiochemistryBiomolecular ElectrostaticsDna StructureElectrostatic Interactions In BiomoleculesElectrostatics In BiomoleculesProtein ConformationProtein StructureBovine Serum AlbuminCompactionDna Compaction MechanismsDna ThermodynamicsElectrostatic RepulsionSalt Concentration EffectsUnfolding KineticsUnfolding Theory
We studied the conformational properties of DNA in a salt solution of the strongly charged protein bovine serum albumin. DNA is compacted when a suitable amount of bovine serum albumin is added to the solution due to a crowding effect and strong electrostatic repulsion between DNA and bovine serum albumin, both of which carry negative charges. However, DNA undergoes an unfolding transition with an increase in the salt concentration. This observation contradicts the current understanding of polymer- and salt-induced condensation, ψ condensation. We propose a simple theoretical model by taking into account the competition between the translational entropy of ions and electrostatic interaction.
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Statistical Physics of Macromolecules
Alexander Y. Grosberg, Alexei R. Khokhlov, H. Eugene Stanley et al. · Computers in Physics · 1995 · 1.7K citations · Full text
Physical Chemistry of Macromolecules
Charles Tanford, Maurice L. Huggins · Journal of The Electrochemical Society · 1962 · 784 citations