ThermodynamicsofProteinFolding

ThermodynamicsofProteinFolding - Thermodynamics of Protein...

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Thermodynamics of Protein Folding Introduction and Literature Review
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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
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Protein Folding Activity of proteins depends on 3-D shape Primary structure Secondary and Tertiary structure
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Amino Acids Nonpolar: vDW forces
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Amino Acids Polar: Hydrogen bonding
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Amino Acids Acid/base: Ion/ion
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pH and Amino Acids
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Primary Structure
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Polar Peptide bonds
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Secondary Structure: H-bonds
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Secondary Structure: H-bonds
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Tertiary Structure
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Thermodynamics of Taq Work from LiCata, et al. Polymerase E. coli Thermus aquaticaus (Taq) Active fragments
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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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Free Energy of Folding
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Free Energy of Folding for Taq Experiment pH 9.5 Guanidinium chloride To compare, need same conditions for both without aggregation of proteins Taq Gunfold = 27 kcal/mol
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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 - Thermodynamics of Protein...

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