1. Proteins… Let’s Review…… then….. Let’s discover proteins…. PollEv.com/tinalambiase209

2. Functions of Proteins … Enzymes – reduces activation energy Ex: amylase – helps to digest amylose ATP synthase – helps to make ATP Structural Proteins – provide support ex: elastin, horn, silk (web), keratin (hair & nails) Movement – actin and myosin muscles Defense – antibodies in bloodstream Storage – albumin in egg whites Signaling – growth hormones in bloodstream

5. What do you think is happening to the proteins within these eggs????

6. Proteins C, H, O, N and sometimes S Made in ribosomes Cell membranes Hormones (insulin) Hemoglobin Enzymes (control the rate of reactions)

7. Proteins Proteins are made of Amino Acids There are 20 different amino acids. Each having a similar general structure - Differ only in their “R” groups

8. Peptide Bonds Amino acids form proteins via dehydration synthesis forming peptide bonds Two amino acids linked together are called dipeptides More than 2 linked together are called polypeptides - polypeptides can be thousands of amino acids long

9. Can you draw a peptide bond? Which two functional groups join to make the peptide bond???

10. Dehydration synthesis of a protein

11. Hydrolysis of a Protein

12. Protein Structure Protein types include globular proteins which are usually enzymes and Fiberous proteins which usually serve for structure (eg. Hair) Proteins Exhibit 4 “levels of structure.

13. Primary Structure Primary Structure of a protein is it’s sequence of amino acids Primary Structure dictates all further levels of protein structure

14. Secondary Structure The Sequence (primary structure) causes parts of a protein molecule to fold into sheets or bend into helix shapes - this is a protein’s Secondary Structure.

15. Tertiary Structure The protein then can compact and twist on itself to form a mass called it’s Tertiary Structure

16. Quaternary Structure Several Proteins then can can combine and form a protein’s Quaternary Structure Various conformations are usually caused by the formation of hydrogen or disulfide bonds. PH, changes or heat can disrupt these bonds, permanently denaturing the protein.