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Carbohydrates

Carbohydrates. Remember “-ose” suffix C, H, O in a 1:2:1 ratio Monomers are MONOSACCHARIDES glucose, fructose, galactose, ribose C 6 H 12 O 6 or (CH 2 O) n /n= 3-8 Isomers: same chemical (molecular) formula but different structural formulas. Monosaccharides. Glucose

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Carbohydrates

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  1. Carbohydrates • Remember “-ose” suffix • C, H, O in a 1:2:1 ratio • Monomers are MONOSACCHARIDES • glucose, fructose, galactose, ribose • C6H12O6 or (CH2O)n /n= 3-8 • Isomers: same chemical (molecular) formula but different structural formulas

  2. Monosaccharides • Glucose • primary, short term energy source • made during photosynthesis

  3. Monosaccharides • Fructose • plant sugar • sweet

  4. Monosaccharides • Ribose • C5H10O5 • Found in ribonucleic acid (RNA) • Deoxyribose • missing an oxygen • Found in DNA

  5. Isomers • Same chemical formula (number and type of atoms) • Different structural formulas (arrangement of atoms in space)

  6. Disaccharides • Two monosaccharides joined together by dehydration synthesis(2 sugars) • Sucrose--table sugar--fructose + glucose • Lactose--milk sugar--glucose + galactose • Maltose--malt sugar--two glucose

  7. Dehydration Systhesis to form Disaccharide

  8. Other Disaccharides

  9. Polysaccharides • Complex • Made of many monosaccharides (glucose is most common) • Condensation Rxn • Glycogen, Chitin (animals) • Starch, Cellulose (plants)

  10. Polysaccharides--Glycogen • Branched chain of glucose monomers • Intermediate energy source for animals • Stored in liver and muscles • Liver converts to glucose through hydrolysis when quick energy is needed

  11. Polysaccharides--Starch • Branching or spiral chain of glucose monomers • Plant storage molecule--energy reserve

  12. Polysaccharides--Cellulose H-Bond • Long straight chains of glucose monomers • Chains laid side by side, connected by Hydrogen bonds • Structural carbohydrate--does not provide energy • “Fiber” • Most abundant carb

  13. Cellulose (SEM)

  14. LIPIDS • C, H, O • Large numbers of C’s and H’s/few O’s • Fats, oils, waxes, steroids • NONPOLAR/HYDROPHOBIC • Excess energy storage (2x’s carbs), insulation, padding and shape, vitamin storage, structural, chemical messengers

  15. Lipid Monomers • Glycerol--3 carbon chain • Fatty acid chain--hydrocarbon (C and H) with a fatty acid (carboxyl group) COOH attached Fatty Acid Chain glycerol

  16. Triglycerides • Type of lipid • glycerol + 3 fatty acids • saturated or unsaturated

  17. (+H2O) Dehydration Syntheis (-H2O)

  18. C-O-C Bridge

  19. Unsaturated Triglyceride • Hydrocarbon portion has one or more double or triple bonds • bent chain (double and triple bonds in FA Chain • plants/liquid at room temperature

  20. Saturated Fatty Acid • Single bonds in hydrocarbon chain • Straight chains • Animals/solid at room temperature • Atherosclerosis (plaques in arteries)

  21. Straight Chain Bent Chain  kinks

  22. Hydrogenation • The process of converting naturally unsaturated oils into saturated ones through the forced addition of hydrogens. • Gets rid of double/triple bonds to create a solid, straight chained fat • Peanut butter and margarine

  23. WAXES • Long chain fatty acids + an alcohol group • long chain makes it very waterproof • Plants use waxes as coating--cuticle--to keep from drying out • Animals use wax as protection against microorganisms--ears

  24. PHOSPHOLIPIDS • Almost like a triglyceride except a phophate group takes the place of one fatty acid chain • Glycerol + 2 FA chains + 1 phosphate group • Head-phosphate-polar • Tail-FA chain-nonpolar

  25. Phospholipid Models

  26. STEROIDS • Four fused carbon rings • 3 six sided, 1-5 sided, and an R goup (variety) • No glycerol or fatty acid • Nonpolar property makes them a lipid R’

  27. PROTEINS • C, H, O, N • Monomer is amino acid (20 different) • Condensation Rxn • Amino Acid has five parts • amine group (NH2), central carbon, carboxyl group (COOH), single hydrogen, R group • R (radical group) determines type of amino acid and properties

  28. Amino Acid Monomer Single H Central C R group R group different in each Amino Acid: 20 Different R groups

  29. Formation of a Peptide (Protein) • Peptide bonds form during condensation • Covalent in nature

  30. Levels of Protein Organization • Primary Structure • straight chain amino acid sequence

  31. Secondary Structure • helical • fomation of hydrogen bonds between amino acids of one primary chain

  32. Tertiary Structure • folding of primary structure occurs • various interactions between atoms of amino acids

  33. Quaternary Structure • association of two or more peptides (proteins) with the primary structure

  34. Functions of Proteins • Used in cell membrane--transport • Enzymes--Catalysts (-ase suffix) • Antibodies--immune system • Hormones • Venom • Structural--muscles

  35. Lock and Key Model of Enzyme • Substrate is reactant being catalyzed (changed) • Fits into enzyme like key fits into lock • Weakening of chemical bonds • Enzymes not altered and can be reused • Substrate specific

  36. How a Poison Works • Poison molecule blocks enzyme so it cannot recognize its substrate • Example: locoweed poisoning in livestock

  37. Denaturing • Heat or weak acid can destroy Hydrogen bonds/inactivates enzymes • tertiary structure will uncoil (denaturation) • vinegar (acetic acid) can “cook” albumen (white) of egg without heat • proteins in raw fish denatured by citric acid in lime or lemon juice • hemolytic proteins at site of snakebite can be denatured by electrical discharge (stun gun)

  38. Nucleic Acids • Polymers that store genetic information • Monomers are nucleotides • 3 parts: phosphate group, sugar (ribose or deoxyribose), and one of four nitrogen bases • DNA: deoxyribose + phosphate + base (adenine, guanine, thymine, cytosine) • RNA: ribose + phosphate + base (adenine, guanine, uracil, cytosine) • Bonding (A-T or A-U; C-G)

  39. C5H10O5 C5H10O4

  40. Purines (2 rings) adenine, guanine Pyrimidines (1 ring) cytosine, thymine, uracil Nitrogen Base Types

  41. Rosalyn Franklin • First to recognize the helix shape of DNA using X-ray crystallography • Her work was passed on to James Watson and Francis Crick who used it to determine the detailed structure of DNA • Never given official credit for her contribution to the study • Died at age 37 from cancer

  42. James Watson and Francis Crick • Used Franklin’s information to determine details of DNA • Won Nobel Prize for discovery in 1962

  43. VERY Helpful Websites • www.emc.maricopa.edu • Choose Biology, then #3 Chem II: Water and Organic Molecules • www.waynesword.palomar.edu/bio100 • Choose Chemicals of Living Systems

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