lecture4 - Course Subsection Outline 1 Amino Acids 2...

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Copyright 2002 University of Florida. All Rights Reserved Course Subsection Outline 1. Amino Acids 2. Peptides and Peptide Bonds 3. Three-dimensional Structure of Proteins 4. Protein Dynamics and Protein Folding 5. Protein Function, Myoglobin and Hemoglobin 6. Protein Function, Contractile and Motile Systems
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Copyright 2002 University of Florida. All Rights Reserved Protein Folding Figure 6.20, p. 182: Biochemistry; Mathews, Van Holde, Ahern See also Figure 6-27, p. 193: Lehninger Principles of Biochemistry Ribonuclease Folding Denature as temperature rises, but completely reversible In this case, the essential structure information is stored in the primary sequence of AA’s
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Copyright 2002 University of Florida. All Rights Reserved Thermodynamics of Protein Folding Free Energy; G = H - T S (- G favors folding) G H S Protein (kJ/mol) (kJ/mol) (kJ/K mol) Ribonuclease -46 -280 -0.790 Lysozyme -62 -220 -0.530 Myoglobin -50 0 +0.170 (@ 25 0 C and pH of maximum stability) Figure 6.22, p. 186: Biochemistry; Mathews, Van Holde, Ahern
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Copyright 2002 University of Florida. All Rights Reserved Factors that Effect Protein Folding Conformational Entropy Change from random coil to single folded structure results in – S hence an increase in G, i.e. folded structure is less random but less favored. Charge-Charge Interactions Oppositely charged side groups can form salt bridges due to electrostatic attractive forces, - H, e.g (+) amino group of lysine attracted to (-) γ -carbonyl of glutamic acid. Lysine O NH 3 + NH 3 + O - Glutamic Acid O O O - O - NH 3 + + Free Energy; G = H - T S (- G favors folding)
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Copyright 2002 University of Florida. All Rights Reserved Internal hydrogen bonding Many side chain groups can act as hydrogen bond donors or acceptors; - H, e.g. OH of serine and C=O or NH2 of asparagine.
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lecture4 - Course Subsection Outline 1 Amino Acids 2...

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