27 - Nature of protein-DNA interactions 27.1 The...

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The intermolecular forces that determine how proteins interact with DNA involve electrostatic interactions, hydrogen bonds sometimes mediated by water molecules, van der Waals interactions, hydrophobic forces and stacking between amino acids and nucleic acid bases. www.bioinfomaster.ulb.ac.be/ English/CourseMaterial/TrRegPresentation3.ppt van der Waals: the term van der Waals interaction refers to a combination of attractive interactions involving induced electronic multipoles (induced dipole-induced dipole) and short-range repulsive interactions due to unfavorable spatial overlap of electron orbitals. Hydrophobic interactions: each hydrophobic molecule (mainly nonpolar solute) when introduced into water provokes the decrease of the entropy of the system ("cage" model). Thus, hydrophobic molecules will tend to self-associate in water, because doing so will decrease their total surface area in contact with the solvent and the unfavorable entropy decrease will be minimized. Aggregation on nonpolar solutes in water is 'entropy-driven'.
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This note was uploaded on 02/23/2011 for the course CHEM 4731 taught by Professor Mchenry during the Spring '08 term at Colorado.

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27 - Nature of protein-DNA interactions 27.1 The...

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