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Biochemistry

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This overview explores the fundamental concepts of biochemistry, focusing on organic molecules, their structures, and functional groups. It highlights the importance of carbon in forming diverse molecules through covalent bonds. The review includes the Miller/Urey experiment, details various functional groups such as carboxyl and amino, discusses amino acids and proteins, and explains their structures, including primary, secondary, tertiary, and quaternary forms. Additionally, it addresses the role of enzymes, isomers, and the processes of building and breaking down macromolecules.

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Biochemistry

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Presentation Transcript

  1. Biochemistry

  2. Organic Molecules • Molecules that have a carbon skeleton and covalent carbon-hydrogen bonds • Can be man made

  3. Carbon • Can form 4 covalent bonds • Allows for molecular diversity in shape and length

  4. Miller/Urey Experiment

  5. Review of Functional Groups • ID the various functional groups in the following molecules…

  6. Phosphate Adenosine

  7. Carboxyl group (COOH) It’s a fatty acid… why acid?

  8. Ethanol… alcohol in adult beverages OH… looks like ____... Alcohol can make you do these types of things…

  9. Alanine Amino  NH2 Carboxyl  COOH (think about what this is going to do when in a solution) What is alanine an example of? There are 20 of them.

  10. Aldehyde • Think… formaldehyde stinks… put it on the end! • Ketone trick?

  11. Proteins • More than 50% of the dry weight of an organism • Made of smaller subunits (monomers) amino acids

  12. Amino Acids • Amino Group • Carboxyl Group • Hydrogen Atom • R group (20 different  different properties)

  13. Proteins • Amino Acids connected by Peptide Bonds • Dipeptide • Polypeptide

  14. Groove (a) A ribbon model Figure 5.19 Protein Structure

  15. Protein Structure • Primary- Chain of amino acids • Secondary- Due to H-Bonds between amino acids

  16. Protein Structure • Tertiary- “Active” Shape • H-Bonds between R-groups • Ionic Bonds between R- groups • Nonpolarity (pushed together by water) • Sulfur bridges (covalent bond between 2 cysteines) • Van der waals attractions

  17. Protein Structure • Quarternary Structure • Joining of two or more polypeptide chains

  18. Groove Figure 5.19 (a) A ribbon model

  19. Directions • Pick up an amino acid sequence, scissors, and tape • Grad JUST the amino acids you will need from the back and 9 water molecules (they’re in sheets of 13 so cut them apart) • Assemble your amino acids showing what must be removed to put your amino acids together • ANSWER THE FOLLOWING 1/GROUP (put both names on)

  20. Questions to turn in at the end of the period • What is the polymer that is created when amino acids are bonded together? • What 2 functional groups are present on EVERY amino acid (name & draw) • If all amino acids share 2 functional groups then why are they different? EXPLAIN. • What reaction must occur in order to break a chain of amino acids into individual amino acids? • What must happen to a chain of amino acids to make it a protein?

  21. Fig. 5.1 Shows all the functions proteins can have:

  22. Groups • Catalysts- Enzymes  speed up rates of chem. rxns • Structural- for support; hair, silk, connective tissue • Storage- source of amino acids for young

  23. Groups • Transport- of other substances • Hormonal- coordinates and directs regulation of organisms • Receptors- decide what comes in/out of cells

  24. Groups • Transcription factors- tells cells what to make • Motor- make up muscles, cilia, flagella, etc • Defensive- antibodies

  25. Enzymes • Organic Catalysts • Lower Activation Energy • May need a coenzyme in order to function

  26. Factors affecting enzymes • Do the Lab!!!

  27. Isomers • Isomers- Molecules with same atoms but different arrangement and properties

  28. Functional Groups • Groups of atoms that give a molecule specific properties

  29. Hydroxyl • Alcohols

  30. Carbonyl • Ketones, formaldehyde

  31. Carboxyl • “Organic” Acids

  32. Amino • Amino Acids

  33. Sulfhydryl • Found in proteins

  34. Phosphate OR • Phospholipids, Nucleotides

  35. Building Macromolecules • Monomers- Small organic molecules that can be linked together • Polymers- Big things (monomers linked together)

  36. Building • Condensation (dehydration synthesis): connects 2 molecules. • One molecule loses an H, the other loses an OH • One water molecule is formed

  37. Taking Apart • Hydrolysis- Breaking down a polymer • Requires a water molecule

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