Biology 1: Molecular Biology; Cellular Respiration -Water: 70% of body, has high boiling point (because of )methane, ethane,

propane, butane, all gases at room temperaturepolar molecule. Breaks down most macromolecules in body through . -Lipids: Low water solubility. Set up hydrophobic/philic regions of cells. Phospholipids - Cell membranes are made with a phosopholipid bilayer. Amphipathic which means Triglycerides Related structure to phosopholipids. Steroids four-ringed. Hormones, help to regulate membrane fluidity, cholesterol, progesterone, testosterone, estrogen. Lipoproteins transport lipids in blood (why?). Density related to composition. Proteins are dense, triglycerides are not, steroids and phospholipids fall in between, so HDLs are higher in protein content, lower in triglycerides, and vice versa for VLDLs. Look at the structures and this should make sense to you. Glycolipids Like phospholipids, except with carbohydrate portion instead of a phosphate group, also amphipathic, involved in cell-cell signaling, found in myelinated cells. -Proteins 20 amino acids, which fall into the following categories: Basic HAL; Acidic Aspartic and Glutamic Acids; Nonpolar VIP MALT Ph Glycine or I saw Lucy methodically probe and feel Alan, then Val tripped Glycine. The rest are polar.

Above is the generic form of an AA. R stands for the alkyl side group, and this is the only place where the alphaamino acids differ. Proline isnt technically an alpha-amino acid. Whats different about it? Primary Structure: Peptide bonds. What kind of bonds? How strong are they? Secondary: Hydrogen bonds. These create pleated sheets and helices. Tertiary: Held together by several forces/bonds, including disulfide bridges between . These are what kind of bonds? Tertiary structure is the folding of the polypeptide. Quaternary: The same forces/bonds as in tertiary structure, only between . Not all proteins have quaternary structure. 3/4 forces/bonds: covalent (disulfide), electrostatic (mostly between acidic and basic residues), hydrogen, Van der Wahls, hydrophobic/philic interactions. Denaturation disrupts which bonds? -Carbohydrates We should be familiar with glucose in its monomeric and polymeric forms. Glucose is a hexose aldose. The anomeric carbon (in the ring structure, it is the only carbon that bonds to two oxygens) has two orientations, and . If you remember that carbon numbering starts with the anomeric carbon, C1, then its no surprise that 1-4 linkages lead to straight chains and 1-6 to branching. Animals can digest alpha linkages, like the ones in starch (potatoes, rice) and glycogen (meat), but only bacteria can digest beta linkages, like in cellulose (greens). -Nucleic Acids A nucleotide is made up of 1) a five carbon sugar (e.g. ribose, deoxyribose), 2) a nitrogenous base, 3) a phosphate group. Jordan: I thought nucleoside meant to kill yourself with a nuclear weaponwhich reminds me of a story: I knew a nitrogenous base. He took a wife, named Ribose. Together, they had three little phosphates. Now, the winter was cold that year, and they lost those little phosphates. And you know, they took that loss real hard. They committednucleoside. page 1 of 2

Biology 1: Molecular Biology; Cellular Respiration -Enzymes Enzymes are highly specific organic catalysts and, like all catalysts, they greatly increase the rate of the reaction that they catalyze, though they remain unchanged, and they do not affect the equilibrium of the reaction. Enzymes are polypeptides, and often work in conjunction with mineral cofactors. Enzymes have an optimal pH and temperature range. -Enzyme Inhibition Imagine the chairs in our class as active sites. If theyre full, weve reached our vmax and other students will have to wait in line to get their learning on. Were at max capacity. Imagine now that we play musical chairs together, teachers vs. students, so me vs. all of you, with just one chair, the active site. If its me vs. one of you, I have a decent chance of winning and thereby keeping you from the active site. But what if youre all playing, or if our class grew. Effectively, one of you would almost always win. I am acting here like a competitive inhibitor, and you have overcome my inhibition by increasing substrate (thats you!) concentration to the point where the reaction rate has effectively returned to the max level (vmax). What if, though, I put some rotten eggs under the chair? That would be like a noncompetitive inhibitor, since the active site is unoccupied, but something about it has changed that allows you to sit in it but makes you less productive. What if I lit the chair on fire? That would be like irreversible inhibition. -Enzyme Regulation Well see examples of these, wherever important. Read this section for background knowledge. -Cellular Metabolism Cellular metabolism of glucose comes in two flavors: anaerobic and aerobic. Glycolysis starts off both. -Glycolysis 6-Carbon Glucose is split into two 3-Carbon Pyruvates. 2 ATP are used, and 4 ATP are produced, for a net 2 ATP. One NADH molecule is also formed for each Pyruvate (for a total of two NADH). -Fermentation In the absence of oxygen (such as, for example, during intense anaerobic exercise), the pyruvates continue through fermentation, which actually encompasses glycolysis. Fermentation in humans reconstitutes the NADH to NAD+ and creates lactic acid from the Pyruvate. Fermentation, including Glycolysis, occurs in the cytosol. -Aerobic Respiration In the presence of oxygen, the pyruvates will enter the mitochondrial matrix to undergo Aerobic Respiration instead of fermentation. An ATP is required to get each NADH into the matrix (though the pyruvate do not), so when we enter the matrix, we have a net ATP production of 0. Lets look at just one pyruvate for now. The Pyruvate enters and is converted to Acetyl CoA (recognize the vitamin cofactor in the name) in a process that creates another NADH. Put that NADH with the other one that came in with this pyruvate. Acetyl CoA goes through a turn of the Krebs Cycle, and produces 1 ATP, 3 NADH and an FADH2. So far, we have, for half of a glucose molecule, 1 net ATP, 5 NADH and 1 FADH2. The ATP produced thus far, including those used up, were all produced through substrate-level phosphorylation (using the energy of phosphorylated compounds), which is not the most efficient of methods. The 5 NADH and 1 FADH2 contain high energy electrons that are passed along cytochromes in the Electron Transport Chain, losing energy along the way to the cytochromes, energy that is used to pump H+ into the intermembrane space, creating a strong gradient that pushes H+ back into the mitochondrion. The end of the chain has ATP-Synthase, which allows the H+ ions to diffuse back in, which makes the top of the ATP synthase spin, the energy of which is captured and used to make ATP from ADP. This is oxidative phosphorylation, which uses the energy of a concentration gradient to form ATP. Notice that all of the reactions in aerobic respiration really just created high energy electrons that were used to create a concentration gradient, not to create ATP directly. The ultimate acceptor of these electrons is O2, which turns into H2O. For each NADH, 3 ATP are produced, and for every FADH2, 2 ATP. Add them up, and each half of glucose forms 18 ATP, for the magic number of 36 for an entire glucose molecule. Also, know that aerobic respiration of glucose is a combustion reaction, and that the overall reaction is: C6H12O6 + O2 CO2 + H2O (unbalanced). page 2 of 2