crystal structures: These structures show that most nonpolar side chains are buried inside a protein, which is tightly packed and which excludes water. If this analogy holds, anything that will promote benzene solubility will lead to increased hydrophobic amino acid side chain exposure to water and hence protein denaturation. Does this also drive protein folding? To explore this questions, we will study the thermodynamics of small nonpolar molecules, especially benzene, with water and ask whether the thermodynamic parameter associated with benzene solubility are similar to those associated with protein stability. We have studied the role of the hydrophobic effect (involving the favorable entropic release of caged water molecules about solvent-exposed hydrophobic groups) in driving micelle and bilayer formation.
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