1. 3.2 Proteins Mini Lecture Radjewski

2. Major functions of proteins: Enzymes—catalytic proteins Defensive proteins (e.g., antibodies) Hormonal and regulatory proteins—control physiological processes Receptor proteins—receive and respond to molecular signals Storage proteins store amino acids Structural proteins—physical stability and movement Transport proteins carry substances (e.g., hemoglobin) Genetic regulatory proteins regulate when, how, and to what extent a gene is expressed

3. Protein monomers are amino acids. Amino and carboxylic acid functional groups allow them to act as both acid and base. The R group differs in each amino acid.

4. Only 20 amino acids occur extensively in the proteins of all organisms. They differ by their R groups.

10. Oligopeptides or peptides—short polymers of 20 or fewer amino acids (some hormones and signaling molecules) Polypeptides or proteins range in size from insulin, which has 51 amino acids, to huge molecules such as the muscle protein titin, with 34,350 amino acids.

11. How to make a protein Amino acids are linked in condensation reactions to form peptide linkages or bonds.

12. Primary structure of a protein—the sequence of amino acids

13. Secondary structure— regular, repeated spatial patterns in different regions, resulting from hydrogen bonding α (alpha) helix— right-handed coil β (beta) pleated sheet—two or more polypeptide chains are extended and aligned

14. Tertiary structure—polypeptide chain is bent and folded; results in the definitive 3-D shape The outer surfaces present functional groups that can interact with other molecules.

15. Interactions between R groups determine tertiary structure. Disulfide bridges hold a folded polypeptide together Hydrogen bonds stabilize folds Hydrophobic side chains can aggregate van der Waals interactions between hydrophobic side chains Ionic interactions

16. Quaternary structure—two or more polypeptide chains (subunits) bind together by hydrophobic and ionic interactions, and hydrogen bonds. These weak interactions allow small changes that aid in the protein’s function.

17. Factors that can disrupt the interactions that determine protein structure (denaturing): Temperature Concentration of H + High concentrations of polar substances Nonpolar substances