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Proteins

Proteins. October 10, 2012. Functions . Building Blocks Structural components of many cells Antibodies Involved in defending the body against foreign invaders. Functions (cont.). Enzymes Catalyze chemical reactions Examples: Amylase and Lactase They can become Denatured

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Proteins

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  1. Proteins October 10, 2012

  2. Functions • Building Blocks • Structural components of many cells • Antibodies • Involved in defending the body against foreign invaders

  3. 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

  4. Functions • Signaling • Cells signal one another • Example: Muscle contraction • Transporters • Bind to molecules and carry them to other cells

  5. 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

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

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

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

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

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

  11. Amino Acids Nonpolar Polar Acidic Basic

  12. 4 Levels of Structure • Primary Structure • A chain of amino acids • Bonds between amino acids are covalent or peptide bonds *NOW IT’S CALLED A POLYPEPTIDE

  13. Polypeptide Bond

  14. Polypeptide Bond (cont.)

  15. 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

  16. Hydrogen Bonding: Alpha and Beta

  17. 4 Levels of Structure (cont.) • Tertiary Structure • 3-D folding of secondary structures • Bonding occurring within the protein due to interaction of R groups Types of R group bonds • Hydrophobic interactions occur between Nonpolar R groups • Ionic Bonds- occur b/w an acid (-) & base (+) • Disulfide bonds- occur b/w 2 cysteine R groups • Hydrogen bonds- occur b/w Polar R groups in which an N, O, or F will be present (some exceptions) • At this stage it is a functional protein

  18. Bonding in Tertiary Structure

  19. 4 Levels of Structure (cont.) • Quaternary Structure • Tertiary proteins bond with each other (2 or more polypeptides bond), so you have a group of proteins bonded together • Example: Hemoglobin

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