102 handout 920 KEY - 1 Draw the approximate positions of...

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MCB102 Handout 9/20 Decreasing MW 1. Draw the approximate positions of these four proteins on a 2D gel. Myoglobin: molecular weight = 16,700 Da pI = 7.0 Lysozyme: molecular weight = 14,400 Da pI = 11.0 Pepsin: molecular weight = 34,000 Da pI < 1.0 Urease: molecular weight = 480,000 Da pI = 5.0 Decreasing pI 2. List the major enthalpic and entropic contributions (positive and negative) to the overall free energy change as a protein folds. Consider both the protein and the aqueous environment. Positive Negative . Enthalpy Breaking of noncovalent interactions Formation of noncovalent between protein and  water (solvent).        interactions between groups within the protein. Entropy Release of water that was ordered Decrease in the conformational around nonpolar regions of the protein. freedom of the protein. Negative enthalpy and positive entropy are energetically favorable. 3. Compare the benefits and drawbacks of X ray crystallography and NMR for determining structure.
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