Protein Structure and Function. Primary Structure  Made of amino acids covalently bonded together.

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Presentation transcript:

Protein Structure and Function

Primary Structure  Made of amino acids covalently bonded together

Secondary Structure Caused By Hydrogen Bonds

Tertiary Structure

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

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

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

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

Quaternary Structure

Hemoglobin Carries Oxygen

Hemoglobin is a different shape with oxygen bound

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

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

Sickle-Cell Hemoglobin

Just 1 Amino Acid Difference Glutamic AcidValine

Effects of Sickle Cell