ThermodynamicsofProteinFolding

ThermodynamicsofProteinFolding - 11/18/2011 Thermodynamics...

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11/18/2011 1 Thermodynamics of Protein Folding Introduction and Literature Review Overview Applications of what we have learned Intermolecular forces Effect of acid/base chemistry Calorimetry Free energy of folding Equilibrium and stability of solvation Entropy: The hydrophobic effect Protein Folding Activity of proteins depends on 3 D shape Primary structure Secondary and Tertiary structure
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11/18/2011 2 Amino Acids Nonpolar: vDW forces Amino Acids Polar: Hydrogen bonding
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11/18/2011 3 Amino Acids Acid/base: Ion/ion pH and Amino Acids Primary Structure
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11/18/2011 4 Polar Peptide bonds Secondary Structure: H bonds Secondary Structure: H bonds
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11/18/2011 5 Tertiary Structure Thermodynamics of Taq Work from LiCata, et al. Polymerase E. coli Thermus aquaticaus (Taq) Active fragments Klenow Klentaq Calorimetry of Taq Differential Scanning Calorimetry measures difference in energy needed to keep sample and reference increasing in temperature Marks energy input into non kinetic mode (degree of freedom) H = C T
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11/18/2011 6 Free Energy of Folding Free Energy of Folding for Taq Experiment pH 9.5 Guanidinium chloride To compare, need same conditions for both without
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This note was uploaded on 01/18/2012 for the course CHEM S117 taught by Professor Desouza during the Fall '10 term at Indiana.

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ThermodynamicsofProteinFolding - 11/18/2011 Thermodynamics...

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