1. FCAT Biology Review

3. Poly=many

4. Mono=one

5. Think of a beaded bracelet….

6. each bead is a MONOMER

7. The entire bracelet is a POLYMER

8. Large variety of polymers but there are less than 50 monomers…kinda like the alphabet…lots of words, only 26 letters

9. Three of the four classes of life’s organic molecules are polymers:Carbohydrates Proteins Nucleic acids ***Lipids/fats are not polymers but they are still macromolecules

10. Making and Breaking Polymers Polymerization: making polymers Dehydration Reaction Dehydrate means water loss When a water molecule (H-OH) is released to join a monomer to another monomer Hydrolysis Hydro- water Lysis- to break down Def: to break apart or disassemble a polymer by adding water (H-OH)

11. LE 5-2 Short polymer Unlinked monomer Dehydration removes a water molecule, forming a new bond Longer polymer Dehydration reaction in the synthesis of a polymer Hydrolysis adds a water molecule, breaking a bond Hydrolysis of a polymer

12. Carbohydrates Monomer: Monosaccharide Polymer: Disaccharide or Polysaccharide Link between monomers is called: Glycosidic Linkage Formed by a dehydration reaction Always have Carbon, Hydrogen, and Oxygens CxH2xOx Common name: sugar End with suffix “-ose” Function: Energy/fuel, structure, storage GLUCOSE!!!! What all cells need for energy

13. Carbs continued Monosaccharides Glucose fructose Disaccharides sucrose Polysaccharides Starch In plant cells; chain of glucose molecules coiled up like a phone cord Glycogen Excess sugar in animal cells is stored in this form; highly branched and more complex chain of glucose monomers Stored in muscle and liver cells When body needs energy, glycogen is broken down into glucose Cellulose Found in plant cell walls; made of glucose monomer; building material; aka FIBER; humans do NOT have the enzyme to break this polysaccharide down Passes through digestive tract and keeps it healthy but NOT a nutrient Some animals (cows) have microorganisms that live in their digestive tract that help break down cellulose Carbs are hydrophilic because of hydroxl group (-OH) Dissolve in water making sugary solutions Large carbs (starches and cellulose) do not dissolve Think about your towels and clothes, duh!

14. Proteins Monomer: amino acids 20 amino acids Amine (NH2) and carboxyl (COOH) groups attached to carbon Only thing different is side chain…R-group Polymer: polypeptide chains (proteins) Link between monomers is called: polypeptide bond Made by a dehydration reaction (between amine group of one aa and carboxyl group of another aa) STRUCTURE of A.A. Amino group on one end (-NH2) Carboxyl group on one end (COOH) Hydrogen R-group/side chain (changes) Function of Proteins: structural support Storage Transport cellular communications Movement defense against foreign substances Proteins account for more than 50% of the dry mass of most cells

16. Protein Structure Primary structure 1’ Order of amino acids in a polypeptide chain Secondary structure 2’ Polypeptide chain folds because of interactions between amino acids HYDROGEN BONDING Tertiary Structure 3’ Gives proteins 3-D shape VERY IMPORTANT to function of protein Beta pleated sheets and alpha helices fold based on interactions between R-groups of a.a. Hydrogen bonds, polar/non-polar interactions, acid/base interactions, disulfide bonds, van der Waals forces Quaternary Structure 4’ the association of the polypeptide chains some proteins contain more than one polypeptide chain Each polypeptide chain in the protein is called a subunit Two or more subunits come together for a specific function HEMOGLOBIN On Red blood cells Its shape allows RBCs to carry oxygen all around your body!

17. Denaturation Unraveling/unfolding of protein Why would this be a problem? When protein loses its 3-D shape and thus its specific function Caused by: Unfavorable changes in pH, temperature or other environmental condition Disrupts the interactions between side chains and causes loss of shape Examples: Frying an egg Straightening your hair

20. Fats/Lipids Made of mostly carbon and hydrogen…some oxygen Usually not soluble in water Not a polymer but is made of molecular units Glycerol + 3 Fatty Acids= FAT Linkage is called ESTER linkage Dehydration reaction Function Energy storage Insulation waterproofing

21. Types of Fats Saturated Solid at room temperature Animal fats All the carbons in the fatty acid chains contain the MAXIMUM # of hydrogen atoms around each atom SATURATED with hydrogen Only single bonds in fatty acid chain Unsaturated/polyunsaturated fats Liquid at room temperature Plant oils, fish oils One or more double bonded carbon atoms in fatty acid chain, then it is unsaturated

22. Phospholipids

23. Steroids Chemical messengers Structure 4 fused carbon rings Ex. Cholesterol, testosterone, estradiol Function structural component of mammalian cell membranes resilience and fluidity of human membranes mobilized for the synthesis of steroid hormones protecting the human skin against external irritants and for holding water content Improvement of water balance in human skin Enhanced barrier function for stratum Inhibition of aging of skin Water retention for hair

24. Nucleic Acids Monomer: Nucleotide Structure of a Nucleotide Made of a phosphate group, a sugar (ribose or deoxyribose), and nitrogenous base Polymer: Chain of nucleotides (nucleic acids) Deoxyribonucleic acid (DNA) Ribonucleic Acid (RNA) Function DNA genetic instructions used in the development and functioning of all known living organisms Instructions to make RNA and proteins long-term storage of information NITROGENOUS BASES: Pyrimidines: cytosine and thymine Purines: guanine and adenine A binds to T and G binds to C in the polymer DNA RNA messenger between DNA and the protein synthesis complexes known as ribosomes essential carrier molecule for amino acids to be used in protein synthesis Three types: mRNA, tRNA, rRNA NITROGENOUS BASES: Pyrimidines: cytosine and uracil Purines: guanine and adenine A binds to U and G binds to C in the polymer RNA

27. 20 Activation Energy The minimum amount of energy necessary to get a reaction going is called the activation energy, EA. All reactions have a certain amount of activation energy that must be overcome for the reaction to occur Applet showing collision of particles with different energy (<EA and > or = EA) and orientation.

28. 21 Exothermic Reaction and EA Before the reaction gets to the lower level of the products, it must get over the hump of the activation energy.

29. 22 Endothermic Reaction and EA For the reaction to get to the higher energy level of the products, the activation energy must be supplied and stored in the bonds of the products.

30. 23 Activation Energy Affects the Rate of a Reaction The greater the required activation energy of a reaction, the slower the reaction will proceed. If the required activation energy is lowered, a reaction will proceed faster.

31. 24 Catalysts A catalystis a substance that makes a reaction go faster by lowering the required activation energy. AcatalystIS NOT changed or used up in a reaction.

32. 25 Effect of a Catalyst The blue line represents a reaction without a catalyst. The red line represents a reaction where a catalyst was added. The activationenergy is lower so the reaction will go faster.

33. Enzymes Enzyme Catalyst Anything that speeds up the rate of a reaction by lowering the ACTIVATION ENERGY Activ. E: energy required for a chem. Rxn to start making products used to regulatethe rate (speed) of chemical reactions Protein that helps speed up a reaction that occurs in a biological system Name of enzymes end in –ASE all enzymes are proteins, but not all proteins are enzymes each chemical reaction in an organism requires its own specific enzyme enzymes are never changed by their reactions! Substrate Molecule/compound that attaches to enzyme Active Site Specific location on enzyme for substrate to attach Where the enzymatic reaction occurs Enzyme-substrate complex When substrate binds to active site of enzyme Products molecules produced at the end of an enzymatic reaction

34. Factors that Effect the Rate of Reactions Temperature Hot Breaks bonds that give proteins its tertiary structure DENATURES Cold Slow down chemical reaction (formation of enzyme substrate complex) pH Acids and bases produce OH- and H+ ions too many ions are present, the enzyme may be denatured (twisted and pulled so out of shape that it can no longer function) Inhibitors Non-competitive react with portions of the active site, changing of its shape Allosteric Inhibitors Change shape of the enzyme Attach to regulatory site (not active site) and change the shape of the entire enzyme (specifically the active site) Competitive look like substrate, bind to active site, but do not make the intended product

36. Lock and Key Model

37. Ecological Succession Do all ecosystems stay the same all the time? What are some things that cause changes to ecosystems? Natural and unnatural Quickly and slowly

38. Ecosystems are constantly changing in response to human and natural disturbances. As an ecosystem changes, older habitants die out and new organisms move in, causing more change

39. Ecological Succession Series of predictable changes that occur in a community over time Physical environment Natural disturbance Human disturbance

40. Primary Succession Succession on land that occurs on surfaces where no soil exists Volcanic eruptions Glaciers melting

43. Stages of Primary Succession Start with no soil, just ash and rock First species to populate this area “pioneer species” For example, pioneer species on volcanic rock are lichens (LY-kunz) Lichens made up of fungus and algae that can grow on bare rock When lichens die, they for organic material that becomes soil…now plants can grow

44. Secondary Succession Succession following a disturbance that destroys a community without destroying the soil Natural hurricane fires Human disturbances Farming Forest clearing