Chemistry 104

Lecture #16: Proteins

Read pg. 562-567, 570 (section 21.4 and 21.5), 575(section 21.7-21.11), 587(section 21.13)-592, 747(section 27.3)-750

HW: pg. 592 (1a-e, 2, 4, 6, 7, 8, 11, 13, 14, 19, 26, 28, 33-35, 37, 42, and 43 or 47).

Objectives:

  1. Recognize names and abbreviations of all 20 amino acids.
  2. Know the structure and distinctive features of your 3 favorite amino acids.
  3. Be able to draw structures of peptides using a table of amino acids.
  4. Recognize nonpolar, polar but neutral, acidic and basic amino acids.
  5. Explain primary (1o), secondary(2o) (eg proteins in silk are mostly beta pleated sheets while proteins in wool are coiled alpha helices) , tertiary(3o) and quaternary (4o) structure of proteins.
  6. Identify the 4 types of forces that maintain 3o structure of a protein (figure 21.12, pg. 580).
  7. Know the difference between fibrous proteins (insoluble in water, serve structural, connective and protective functions. Examples: keratin, collagen, myosin) and globular proteins (water soluble, spherical. Examples: casein in milk, albumin found in egg whites and plasma).
  8. Know how to denature a protein.
  9. Know that an essential amino acid must be supplied in the diet. Know the consequences of a diet deficient in essential amino acids.
  10. Know definitions for amide linkage, peptide pond, peptide, polypeptide, protein