1. Protein Structure and Function

2. Primary Structure  Made of amino acids covalently bonded together

3. Secondary Structure Caused By Hydrogen Bonds

4. Tertiary Structure

5. To Illustrate 3-d Structure  Toobers!  In group of 4 you will try to assemble your toober  Follow the directions on the sheet to put tacks in the toober- each tack represents a particular type of side chain  As a group think about how each side chain would interact

6. General Shape Guidelines  Non-polar residues should be found on the inside if it is in water  + and δ+ residues interact with – and δ- residues  Two Sulfur containing residues can form a stronger, covalent bond

7. Do All Your Structures Look the Same?  Different foldings are possible (e.g. prions)  Chaperone proteins help fold into correct shape  We don’t fully understand how or why they always take correct shape or lose shape  Lots of diseases associated with incorrect shape

8. More Practice  Build a molecule of any shape  Add amino acids (tacks) that would give it this shape  10 minutes to build then quickly share with class

9. Quaternary Structure

10. Hemoglobin Carries Oxygen

11. Hemoglobin is a different shape with oxygen bound

12. Change of Shape is Critical  In lungs conditions cause hemoglobin to bind oxygen  Near muscles conditions cause hemoglobin to release oxygen

13. What if an Amino Acid is Changed?  Change one amino acid in your protein and as a group discuss what happens

14. Sickle-Cell Hemoglobin

15. Just 1 Amino Acid Difference Glutamic AcidValine

17. Effects of Sickle Cell