1. Biochemistry

2. Outline Non-covalent interactions Thermodynamics
Amino acids & the peptide bond
pH and titration curves
Enzymes (catalysis, kinetics, inhibition)

3. Non-covalent interactions
Van der Waal’s (aka LDF)
Electrostatic
Dipole dipole
Ion-dipole
Ion-ion
Hydrogen Bonding

4. Thermodynamics Bond formation ∆H = always (-) ∆S = always (-)
∆G = (+) or (-), depending on magnitude of ∆H, T∆S
∆G = ∆H – T∆S

5. Amino Acids

6. The Peptide Bond

7. Protein Structure Structure Definition Interactions 1˚
Sequence of amino acids
Peptide bonds (covalent) 2˚
-Bends in the backbone (α helix, ß sheets, loops & turns)
-local structure (close together in a.a. sequence)
Hydrogen bonding of backbone 3˚
Far away in a.a. sequence, close together in 3D space (single polypeptide chain)
Hydrogen bonding
Electrostatics
Van der Waal’s
Disulfides
Hydrophobic effect 4˚
Two or more polypeptide chains interacting
Same as 3˚

9. antiparallel
parallel

11. pH and titration curves

12. Enzymes

13. Active Site: Substrate Specificity

14. Enzyme Kinetics

16. Cooperativity

19. Inhibition

20. Reaction Coupling
A + PO42-  APO42- ∆G = +2 kcal/mol APO42- + B  C + PO42- ∆G = +5 kcal/mol ___________________________________ Total ∆G = +7 kcal/mol These reactions will not proceed! (+∆G)

21. Reaction Coupling ATP  ADP + PO42- ∆G = -12 kcal/mol
A + PO42-  APO ∆G = +2 kcal/mol
APO42- + B  C + PO ∆G = +5 kcal/mol
___________________________________
Total ∆G = -5 kcal/mol
A + B + ATP  C + ADP + PO ∆G = -5 kcal/mol

22. Other AWESOME Biochemistry Topics
Protein folding!
Metabolism!
Signal Transduction pathways!
Allosteric Regulation!
Glycolysis & Gluconeogenesis!
ETC & ATP Synthase!

23. Biochemistry  CHEMISTRY
IMF
Thermodynamics
pH and titration curves
Reaction Coupling