09 - removed form the aqueous environment is worth ~3K/mol...

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12/1/09 Biochemsitry Hydrophobic Forces ∆H -T∆S ∆G CH 4 in H 2 O CH 4 in benzene 117 -22.6 -10.9 What happens when we introduce a nonpolar substance in H 2 O? H 2 O CANNOT H-bond to hydrocarbons H 2 O must rearrange to accommodate the hydrophobic intruder # of ways H 2 O molecules can form H-bonds around the nonpolar substance is less than the # of ways it could H-bond in bulk water Non-polar molecules are forced to aggregate (“squeezing out”) Surface area of aggregate is less than the surface area of its components Hydrophobic bonding No directionality Important in stabilization of proteins Each CH 2
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Unformatted text preview: removed form the aqueous environment is worth ~3K/mol stabilization energy Disulfide linkages are important to extracellular proteins Quaternary Structure Most proteins contain multiple subunits often identical Hemoglobin 4 subunits Why compose a protein of multiple subunits? 1) Easier to synthesize a large protein from several identical pieces 2) Repair easier to repair one defective subunit than an entire protein 3) Large proteins are better suited to unusual conformations 4) Multiple active sites mechanisms to regulate enzymatic activity...
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This note was uploaded on 09/19/2011 for the course CHEM 43 taught by Professor Therien during the Fall '09 term at Duke.

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