AP Biology

1. AP Biology Cellular Biology

2. Chapter 4 Carbon and the Molecular Diversity of Life

3. Figure 4.5 (c) Double bond position (a) Length Ethane Propane 2-Butene 1-Butene (b) Branching (d) Presence of rings Benzene 2-Methylpropane (isobutane) Butane Cyclohexane

4. Figure 4.8 Ineffective Enantiomer Effective Enantiomer Drug Condition Pain;inflammation Ibuprofen S-Ibuprofen R-Ibuprofen Albuterol Asthma R-Albuterol S-Albuterol

5. Figure 4.UN02 Estradiol Testosterone

6. Figure 4.9a Hydroxyl STRUCTURE Alcohols (Their specific names usually end in -ol.) NAME OF COMPOUND (may be written HO—) • Is polar as a result of the electrons spending more time near the electronegative oxygen atom. EXAMPLE FUNCTIONALPROPERTIES Ethanol • Can form hydrogen bonds with water molecules, helping dissolve organic compounds such as sugars.

7. Carbonyl Figure 4.9b STRUCTURE Ketones if the carbonyl group is within a carbon skeleton NAME OF COMPOUND Aldehydes if the carbonyl group is at the end of the carbon skeleton EXAMPLE • A ketone and an • aldehyde may be • structural isomers • with different properties, • as is the case for • acetone and propanal. FUNCTIONALPROPERTIES • Ketone and aldehyde • groups are also found • in sugars, giving rise • to two major groups • of sugars: ketoses • (containing ketone • groups) and aldoses • (containing aldehyde • groups). Acetone Propanal

8. Carboxyl Figure 4.9c STRUCTURE Carboxylic acids, or organic acids NAME OF COMPOUND • Acts as an acid; can donate an H+ because the covalent bond between oxygen and hydrogen is so polar: EXAMPLE FUNCTIONALPROPERTIES Acetic acid Nonionized Ionized • Found in cells in the ionized form with a charge of 1– and called a carboxylate ion.

9. Amino Figure 4.9d Amines STRUCTURE NAME OF COMPOUND •Acts as a base; can pick up an H+ from the surrounding solution (water, in living organisms): EXAMPLE FUNCTIONALPROPERTIES Glycine Ionized Nonionized •Found in cells in the ionized form with a charge of 1.

10. Sulfhydryl Figure 4.9e Thiols STRUCTURE NAME OF COMPOUND (may be written HS—) •Two sulfhydryl groups can react, forming a covalent bond. This “cross-linking” helps stabilize protein structure. EXAMPLE FUNCTIONALPROPERTIES •Cross-linking of cysteines in hair proteins maintains the curliness or straightness of hair. Straight hair can be “permanently” curled by shaping it around curlers and then breaking and re-forming the cross-linking bonds. Cysteine

11. Figure 4.9f Phosphate Organic phosphates STRUCTURE NAME OF COMPOUND EXAMPLE •Contributes negative charge to the molecule of which it is a part (2– when at the end of a molecule, as at left; 1– when located internally in a chain of phosphates). FUNCTIONALPROPERTIES Glycerol phosphate •Molecules containing phosphate groups have the potential to react with water, releasing energy.

12. Figure 4.9g Methyl STRUCTURE Methylated compounds NAME OF COMPOUND •Addition of a methyl group to DNA, or to molecules bound to DNA, affects the expression of genes. EXAMPLE FUNCTIONALPROPERTIES •Arrangement of methyl groups in male and female sex hormones affects their shape and function. 5-Methyl cytidine

13. Chapter 5 The Structure and Function of Large Biological Molecules

14. Figure 5.4 6 6 1 2 5 5 3 4 1 4 1 4 2 2 5 3 3 6 (a) Linear and ring forms 6 5 4 1 2 3 (b) Abbreviated ring structure

16. Hydrolysis

17. Dehydration Synthesis

18. Figure 5.7b 1 4 (b) Starch: 1–4 linkage of  glucose monomers 1 4 (c) Cellulose: 1–4 linkage of  glucose monomers

19. Cellulosemicrofibrils in aplant cell wall Cell wall Figure 5.8 Microfibril 10 m 0.5 m Cellulosemolecules  Glucosemonomer

20. Figure 5.9a Chitin forms the exoskeletonof arthropods.

21. Figure 5.9b Chitin is used to make a strong and flexible surgical thread that decomposes after the wound or incision heals.

22. Choline Figure 5.12a Hydrophilic head Phosphate Glycerol Fatty acids Hydrophobic tails (a) Structural formula (b) Space-filling model

23. Ester linkage Figure 5.10b (b) Fat molecule (triacylglycerol)

24. Figure 5.11 (b) Unsaturated fat (a) Saturated fat Structuralformula of asaturated fatmolecule Structuralformula of anunsaturated fatmolecule Space-fillingmodel of stearicacid, a saturatedfatty acid Space-filling modelof oleic acid, anunsaturated fattyacid Cis double bondcauses bending.

25. Figure 5.13 WATER Hydrophilichead Hydrophobictail WATER

26. Figure 5.15-a Enzymatic proteins Defensive proteins Function: Protection against disease Function: Selective acceleration of chemical reactions Example: Digestive enzymes catalyze the hydrolysisof bonds in food molecules. Example: Antibodies inactivate and help destroyviruses and bacteria. Antibodies Enzyme Virus Bacterium Storage proteins Transport proteins Function: Storage of amino acids Function: Transport of substances Examples: Hemoglobin, the iron-containing protein ofvertebrate blood, transports oxygen from the lungs toother parts of the body. Other proteins transportmolecules across cell membranes. Examples: Casein, the protein of milk, is the majorsource of amino acids for baby mammals. Plants havestorage proteins in their seeds. Ovalbumin is theprotein of egg white, used as an amino acid sourcefor the developing embryo. Transportprotein Amino acidsfor embryo Ovalbumin Cell membrane

27. Figure 5.15-b Hormonal proteins Receptor proteins Function: Response of cell to chemical stimuli Function: Coordination of an organism’s activities Example: Receptors built into the membrane of anerve cell detect signaling molecules released byother nerve cells. Example: Insulin, a hormone secreted by thepancreas, causes other tissues to take up glucose,thus regulating blood sugar concentration Receptorprotein Signalingmolecules Insulinsecreted Highblood sugar Normalblood sugar Structural proteins Contractile and motor proteins Function: Support Function: Movement Examples: Motor proteins are responsible for theundulations of cilia and flagella. Actin and myosinproteins are responsible for the contraction ofmuscles. Examples: Keratin is the protein of hair, horns,feathers, and other skin appendages. Insects andspiders use silk fibers to make their cocoons and webs,respectively. Collagen and elastin proteins provide afibrous framework in animal connective tissues. Actin Myosin Collagen Muscle tissue Connectivetissue 100 m 60 m

28. Figure 5.19 Antibody protein Protein from flu virus

30. Primary structure Figure 5.20a Aminoacids Amino end Primary structure of transthyretin Carboxyl end

31. Secondary structure Figure 5.20c  helix Hydrogen bond  pleated sheet  strand, shown as a flatarrow pointing towardthe carboxyl end Hydrogen bond

32. Figure 5.20e Tertiary structure Transthyretinpolypeptide

33. Figure 5.20f Hydrogenbond Hydrophobicinteractions andvan der Waalsinteractions Disulfidebridge Ionic bond Polypeptidebackbone

34. Heme Iron Figure 5.20i  subunit  subunit  subunit  subunit Hemoglobin

35. Figure 5.20h Collagen

36. Figure 5.22 tu r a a n t i De on Denatured protein Normal protein Re on n i a t a t r u

37. 1 DNA Figure 5.25-1 Synthesis ofmRNA mRNA NUCLEUS CYTOPLASM

38. 1 2 DNA Figure 5.25-2 Synthesis ofmRNA mRNA NUCLEUS CYTOPLASM mRNA Movement ofmRNA intocytoplasm

39. 1 2 3 DNA Figure 5.25-3 Synthesis ofmRNA mRNA NUCLEUS CYTOPLASM mRNA Movement ofmRNA intocytoplasm Ribosome Synthesisof protein Aminoacids Polypeptide

40. Sugar-phosphate backbone 5 end Figure 5.26ab 5C 3C Nucleoside Nitrogenousbase 5C 1C Phosphategroup 3C Sugar(pentose) 5C 3C (b) Nucleotide 3 end (a) Polynucleotide, or nucleic acid

41. Pyrimidines Purines Nitrogenous bases Figure 5.26c Cytosine (C) Uracil (U, in RNA) Thymine (T, in DNA) Sugars Deoxyribose (in DNA) Ribose (in RNA) Adenine (A) Guanine (G) (c) Nucleoside components

42. Figure 5.27 5 3 Sugar-phosphatebackbones Hydrogen bonds Base pair joinedby hydrogenbonding Base pair joinedby hydrogen bonding 5 3 (b) Transfer RNA (a) DNA

43. Chapter 6 A Tour of the Cell

44. Surface Area to Volume

45. Light Microscopy (LM) Electron Microscopy (EM) Cross sectionof cilium Longitudinal sectionof cilium Brightfield Confocal Figure 6.3 (unstained specimen) Cilia 50 m Brightfield (stained specimen) 50 m 2 m 2 m Transmission electronmicroscopy (TEM) Scanning electronmicroscopy (SEM) Deconvolution Phase-contrast 10 m Differential-interference-contrast (Nomarski) Super-resolution Fluorescence 1 m 10 m

46. TECHNIQUE Figure 6.4a Homogenization Tissuecells Homogenate Centrifugation

47. TECHNIQUE (cont.) Centrifuged at1,000 g(1,000 times theforce of gravity)for 10 min Figure 6.4b Supernatantpoured intonext tube Differentialcentrifugation 20,000 g 20 min 80,000 g 60 min Pellet rich innuclei andcellular debris 150,000 g 3 hr Pellet rich inmitochondria(and chloro-plasts if cellsare from a plant) Pellet rich in“microsomes” Pellet rich inribosomes

48. Fimbriae Figure 6.5 Nucleoid Ribosomes Plasmamembrane Bacterialchromosome Cell wall Capsule 0.5 m Flagella (b) (a) A thin sectionthrough thebacterium Bacilluscoagulans (TEM) A typicalrod-shapedbacterium

49. Nucleus Nucleolus Figure 6.9a Chromatin Nuclear envelope: Inner membrane Outer membrane Nuclear pore Rough ER Porecomplex Ribosome Close-upof nuclearenvelope Chromatin

50. Figure 6.11a Smooth ER Nuclearenvelope Rough ER ER lumen Transitional ER Cisternae Ribosomes Transport vesicle