1. Physical-chemical properties of proteins; precipitation reactions

3. Categories of Amino Acid R-groups

4. Essential amino acids Definition - Those amino acids that cannot be synthesized in the body in sufficient quantities for anabolic needs. In humans: Phenylalanine ValineThreonine Tryptophan IsoleucineMethionine Histidine* Arginine*Leucine Lysine *may only be essential for children

5. Peptide bond formation condensation

6. Protein Structure Primary structure is the amino acid sequence. Secondary structure is how the amino acids in sequence fold up locally. Commons examples are  -helixes and  -strands. Tertiary structure is the 3-dimensional folding of the secondary structural elements and connecting loops in space. Quaternary structure is the association of multiple subunits, each with a tertiary structure and each a separate gene product.

7. Dipeptide Peptide bond resonance Primary Structure

8. 2 o structure:  -helixes Intra-chain H-bonds

9. 2 o structure:  -strands Inter-chain H-bonds

10. Tertiary and Quaternary Structures 3 o 4 o Hb monomer (or myoglobin) HbA  2  2 tetramer (multimeric)

11. Stabilization of Protein Structure Electrostatic interactions involve the interaction of (+) and (-) charged (side) groups. Hydrogen bonds involve sharing of a hydrogen atom between two eletronegative atoms (e.g., O, N). Van der Waal’s forces are weak forces based on optimal overlap of adjacent electronic orbitals. Hydrophobic interactions are, by far, the most powerful force stabilizing protein structure. Basis of force is entropy gain realized by burying hydrophobic residues.