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Proteins

Proteins. October 9, 2012. Functions (cont.). Enzymes Catalyze chemical reactions Examples: Amylase and Lactase They can become Denatured When they lose their function and shape in extreme conditions Examples: milk souring, cooking eggs. D. B. C. Structure .

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Proteins

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  1. Proteins October 9, 2012

  2. Functions (cont.) Enzymes • Catalyze chemical reactions • Examples: Amylase and Lactase • They can become Denatured • When they lose their function and shape in extreme conditions • Examples: milk souring, cooking eggs

  3. D B C Structure • Made up of monomer units called… • Amino Acids • Bonded together through the process of….. • Dehydration Synthesis • Break polymers up through process of… • Hydrolysis A

  4. Macromolecule Units Review • Monomer • Smallest unit of macromolecule • Polymer • Formed when many monomers bond

  5. How do you make Macromolecules? • Dehydration Synthesis • Polymers are formed by removing water from monomers

  6. How do you break a macromolecule? • Hydrolysis • Polymers are broken apart by adding water to break up into monomers

  7. Functional Groups Commonly Present • Amino Group • Carboxyl Group

  8. Amino Acid Structure • Each Amino Acid has a different combination of elements labeled simply as its “R Group” • 20 total

  9. Amino Acids Nonpolar Polar Acidic Basic

  10. 4 Levels of Structure • Primary Structure • A chain of amino acids • Bonds between amino acids are nonpolar covalent or peptide bonds

  11. C forms nonpolar covalent bonds because of the arrangement of atoms around it. • It forms four bonds, so the charge is spread out equally • C-H is also a nonpolar bond (on nonpolaramino acids)

  12. Polypeptide Bond

  13. Polypeptide Bond (cont.)

  14. 4 Levels of Structure (cont.) • Secondary Structure • Arrangement of polypeptide bonds into different formations • Alpha helix: Coil or corkscrew formation • Beta Sheet: Pleats or folds • Random Coils • Hydrogen bonding present

  15. Hydrogen Bonding: Alpha and Beta

  16. 4 Levels of Structure (cont.) • Tertiary Structure • 3-D folding of secondary structures • Bonding occurring within the protein • Hydrophobic interactions occur • Ionic Bonds • Disulfide bonds • Hydrogen bonds • At this stage it is a functional protein

  17. Bonding in Tertiary Structure

  18. 4 Levels of Structure (cont.) • Quaternary Structure • Tertiary proteins bond with each other, so you have a group of proteins bonded together • Example: Hemoglobin

  19. Levels of Protein Structure

  20. Levels of Protein Structure

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