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ie. amino acid  peptide  polypeptide  protein

ie. amino acid  peptide  polypeptide  protein. larger. smaller. + H 2 O. +. + H 2 O. +. Dehydration synthesis/condensation reaction. Dehydration Synthesis. Hydrolysis. Hydrolysis reaction. Carbohydrates. Differ in position & orientation of glycosidic linkage.

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ie. amino acid  peptide  polypeptide  protein

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  1. ie. amino acid  peptide  polypeptide  protein larger smaller

  2. + H2O + + H2O +

  3. Dehydration synthesis/condensation reaction

  4. Dehydration Synthesis

  5. Hydrolysis

  6. Hydrolysis reaction

  7. Carbohydrates Differ in position & orientation of glycosidic linkage • Fueland building material • Include simple sugars (fructose) and polymers (starch) • Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH2O • monosaccharide disaccharide  polysaccharide • Monosaccharides = monomers (eg. glucose, ribose) • Polysaccharides: • Storage (plants-starch, animals-glycogen) • Structure (plant-cellulose, arthropod-chitin)

  8. . • Carbohydrates are made of carbon, hydrogen, and oxygen. • Carbohydrates include sugars and starches. • Monosaccharides are simple sugars. • Polysaccharides include starches, cellulose, and glycogen.

  9. The structure and classification of some monosaccharides

  10. Polymer (starch) Starch is a polymer of glucose monomers that often has a branched structure. Polymer (cellulose) Cellulose is a polymer of glucose monomers that has a straight, rigid structure monomer • Carbohydrates can be broken down to provide energy for cells. • Some carbohydrates are part of cell structure.

  11. The polysaccharide cellulose is a major component of the tough wall of plant cells Like starch, cellulose is a polymer of glucose, but the glycosidic linkages differ Cellulose in human food passes through the digestive tract as insoluble fiber Some microbes use enzymes to digest cellulose Many herbivores, from cows to termites, have symbiotic relationships with these microbes

  12. Glycogen

  13. Glycogen is a storage polysaccharide in animals Humans and other vertebrates store glycogen mainly in liver and muscle cells

  14. Chitin, another structural polysaccharide, is found in the exoskeleton of arthropods Chitin also provides structural support for the cell walls of many fungi

  15. The structureof the chitinmonomer Figure 5.9 Chitin forms the exoskeletonof arthropods. Chitin is used to make a strong and flexiblesurgical thread that decomposes after thewound or incision heals.

  16. Storage polysaccharides of plants (starch) and animals (glycogen)

  17. Proteomics: Analysis of proteins and sequences

  18. I. Proteins Myoglobin protein • “Proteios” = first or primary • 50% dry weight of cells • Contains: C, H, O, N, S

  19. Protein Functions (+ examples)? • Enzymes (lactase) • Defense (antibodies) • Storage (milk protein = casein) • Transport (hemoglobin) • Hormones (insulin) • Receptors • Movement (motor proteins) • Structure (keratin)

  20. Overview of protein functions

  21. Overview of protein functions

  22. Four Levels of Protein Structure • Primary • Amino acid (AA) sequence • 20 different AA’s • peptide bonds link AA’s

  23. Amino Acid • R group = side chains • Properties: • hydrophobic • hydrophilic • ionic (acids & bases) • “amino” : -NH2 • “acid” : -COOH

  24. Four Levels of Protein Structure (continued) • Secondary • Gains 3-D shape (folds, coils) by H-bonding • Alpha (α) helix, Beta (β) pleated sheet

  25. Basic Principles of Protein Folding Hydrophobic AA buried in interior of protein (hydrophobic interactions) Hydrophilic AA exposed on surface of protein (hydrogen bonds)

  26. Four Levels of Protein Structure (continued) • Tertiary • Bonding between side chains (R groups) of amino acids • H bonds, ionic bonds, disulfide bridges, hydrophobic interactions, van der Waals interactions

  27. Four Levels of Protein Structure (continued) • Quaternary • 2+ polypeptides bond together

  28. amino acids  polypeptides  protein • Bonding (ionic & H) can create asymmetrical attractions

  29. Chaperoninsassist in proper folding of proteinsNewly made proteins usually must fold from a linear chain of amino acids into a three-dimensional form.Chaperonins belong to a large class of molecules that assist protein folding, called molecular chaperones. The energy to fold proteins is supplied by adenosine triphosphate (ATP).

  30. Protein structure and function are sensitive to chemical and physical conditions • Unfolds or denatures if pH and temperature are not optimal

  31. change in structure = change in function

  32. Genomics: Analysis of genes and genomes

  33. II. Nucleic Acids Function: store hereditary info

  34. Nucleotides: monomer of DNA/RNA Nucleotide = Sugar + Phosphate + Nitrogen Base

  35. Nucleotide phosphate A – T G – C Nitrogen base 5-C sugar

  36. Information flow in a cell:DNA  RNA  protein

  37. II. Lipids Hydrophilic head Hydrophobic tail • Fats (triglyceride): store energy • Glycerol + 3 Fatty Acids • saturated, unsaturated, polyunsaturated • Steroids: cholesterol and hormones • Phospholipids: lipid bilayer of cell membrane • hydrophilic head, hydrophobic tails

  38. The structure of a phospholipid

  39. Hydrophobic/hydrophilic interactions make a phospholipid bilayer

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