BIOL 101 1st EditionFinal Exam Study Guide: Lectures: 1 – 22Chapters 1 – 8, 10, 12 – 17Final Exam FormatThere is a cumulative section that makes up approximately 150 points of the exam, and the second section is based on the material covered post-exam 3. The exam is mostly multiple choice, but be prepared for short answer questions regarding short answer questions covered on previous exams, and any potential drawings. Any matching sections will be solely based on vocabulary. Be able to draw: two functional groups, two water molecules bonded, a phospholipid bilayer, an animal cell, a plant cell, cells undergoing metaphase (meiosis and mitosis), and a complementary strand of DNA.If a student’s score on the final exam is better than that student’s final average in the class (exam 1, exam 2, exam 3, plus any extra credit), then the student’s score on the final exam will be his or her final grade for the semester.Cumulative Section (approximately 150 points)Exam 1 (Lectures 1 – 7): Chapters 1 – 71) Molarity problem, pH problemMolarity is the number of molecules in a given amount of solution. pH is the degree of acidity based on the numbers 0 – 14;7 is neutral, 0 – 6 is acidic, and 8 – 14 is basic.Molarity = number of moles/1 Liter of solutionpH = -log[H+]pH = -log[OH-]pH = [H+][OH-] = 10-14pH + pOH = 142) Valence and bonding questions: What is valence? What is a covalent bond? What is the difference between a polar covalent bond and a nonpolar covalent bond? Name and be able to draw two functional groups that confer polarity to the carbon backbone. What is a hydrocarbon? Explain why hydrocarbons are nonpolar.Valence is the number of electrons needed to fill the outermost orbital shell of an atom.A covalent bond is a bond in which atoms share their electrons.Polar covalent bonds occur when electrons aren’t shared equally between atoms because of differing electronegativities.A nonpolar covalent bond occurs when atoms of equal electronegativity share their electrons equally.Hydroxyl and carbonyl are two functional groups that confer polarity to a carbon backbone. Hydroxyl: R ↔ O ↔ HCarbonyl: R ↔ C ⇔ O ↕ HHydrocarbons are molecules that contain only carbon and hydrogen. They are nonpolar molecules that don’t dissolve in water. Carbon and hydrogen are too close in electronegativity to create polarity in hydrocarbons.3) What is a hydrogen bond? Draw two water molecules and show the hydrogen bond that might form between them (use an arrow to point to the bond). Name two processes in biology where hydrogen bonding is important.Hydrogen bonds are bonds created between a positively charged hydrogen atom of one molecule and a negatively charged atom of another.Hydrogen bonding is important in the structure of amino acids. Hydrogen bonding causes the repeating twisting and folding of the peptide backbone. Hydrogen bonding is also important in DNA. Base pairing, the association of adenine with thymine and cytosine with guanine, is caused by hydrogenbonding, and these base pairs make-up the uprights of the “ladder” in the structure of DNA.4) Be able to name and recognize the four classes of macromolecules. Be able to draw a circle around onemonomer and an arrow pointing to the bond that connects monomers in each. Be able to NAME the monomers and the bonds.The four classes of macromolecules are: proteins, nucleic acids, carbohydrates, and lipids.The monomer of proteins is the amino acid, and they are bonded with a peptide bond.Nucleic acids are comprised of nucleotides. They are bonded through phosphodiester bonds. Carbohydrates are made of monosaccharides that are bonded through glycosidic bonds.Lipids are comprised of glycerol and fatty acid tails attached through ester bonds. 5) Understand water balance in plant and animal cells. What would happen to a red blood cell placed in pure water? What would happen to a plant cell in the same circumstance? Why?Isotonic environments, when the concentrations of water are equal in and out of the cell, are ideal for animal cells, but not for plant cells. If a red blood cell were placed in pure water, it would burst trying to create an isotonic environment. If a plant cell were placed in pure water, the cell would absorb the water, creating turgor pressure, which is ideal for the plant cell.6) What is similar about facilitated transport and active transport? What is different about the two processes? Passive transport is the diffusion of a substance across a membrane, while active transport describes the movement of solute against the concentration gradient, requiring a transport protein.7) What is a transport protein and what does it do? What are the two basic kinds of transport proteins and how are they different from one another?Channels and carrier proteins are the two types of transport proteins that aid polar molecules in crossing plasma membranes. Channels provide a hydrophilic tunnel, designed for specific molecules. Carrier proteins hold onto specific molecules and change shape to shuttle them across the membrane.8) Be able to draw a phospholipid bilayer and label the hydrophobic and hydrophilic parts. What does hydrophobic mean? What does hydrophilic mean?Hydrophobic means water-fearing and hydrophilic means water-loving.Exam 2 (Lectures: 8 – 13): Chapters 6, 8 – 109) What is an enzyme? What class of macromolecules does it belong to? What makes it specific for a certain substrate? What does it mean to denature an enzyme? How does denaturation usually affect enzyme activity?Enzymes are biological catalysts made from proteins that speed up chemical reactions in the cell.It belongs to the macromolecule class of “protein.”Enzymes are specific to a certain substrate based on the shape and size of its active site.Denaturing an enzyme occurs when the active site of an enzyme is destroyed, meaning that it loses its ability catalyze reactions.10) What is an allosteric enzyme? An allosteric site? An allosteric activator? An allosteric inhibitor? How do these molecules alter the activity of an allosteric enzyme?An allosteric enzyme usually has more than one subunit, and oscillates between an active form (catalyzes chemical reaction) and an inactive form (doesn’t bind to the substrate or catalyze the reaction). An allosteric site is the place on an enzyme where a molecule that is not a substrate may bind, thus changing the shape of the enzyme and influencing