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42 Cards in this Set
- Front
- Back
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What are the elements of life? |
Carbon, Hydrogen, Oxygen and Nitrogen |
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What are the essential biomolecules? |
Carbohydrates, Lipids, Nucleic Acids and Proteins. |
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List the naming up to 10 |
1. Methane 2. Ethane 3. Propane 4. Butane 5. Pentane 6. Hexane 7. Heptane 8. Octane 9. Nonane 10. Decane |
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List the 8 Functional Groups |
1. Hydrophobic: R-CH3 2. Hydroxyl: R-OH -H 3. Aldehyde: R-C=O =O 4. Ketone: R-C-R 5. Thiols R-SH 6. Phosphate: R-P=O & 3x -O 7. Carboxyl: R-C=O & -OH 8. Amine: R-NH3 |
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List the different Protein Structures & Something about them |
1. Primary Structure: linear polypeptide, held by peptide bonds. 2. Secondary Structure: Result form H-bonds along the backbone. Either alpha helix or beta pleated sheets. 3. Tertiary Structure: Globular proteins, result from R-group interaction. Driven by the hydrophobic effect. 4. Quaternary Structure: More than 1 protein molecule help together. |
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Describe the relationship btw pKa and pH |
When [HA] = [A]. pH=pKa When pKa > pH, A dominates When pKa< pH, HA dominates |
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List the type of Amino Acids |
1. Hydrophobic 2. Neutral Polar 3. Acidic 4. Basic |
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Define Proteonomics
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The study of proteins and their level of function. |
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What is Gel-Filtration vs. PAGE |
Gel-Electrophoresis: Separation by size. Running the molecules through beads. Small move faster than larger ones. -Runs from cathode to anode PAGE: Separation of proteins by size. They are stained with Coosmassie Blue. |
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How does ATP affect enzyme reaction? |
ATP, depending on the class of enzyme can be the driving force of the reaction. |
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What effects does "Delta" G have? |
- "D" G =0 at equilibrium - +ve"D" G=Endergonic Reaction. Energy requiring. Not spontaneous. - -ve"D" G=Exergonic Reaction. Energy releasing. Spontaneous |
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What is the nature of the Active Site? |
-Lock and Key: Original theory that it was a perfect fit. -Now believed to be an induced fit: the active site changes upon the substrate binding. It is a malleable structure. |
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Define: Enzyme Kinetics, Vmax and KM |
Enzyme Kinetics: The study of enzyme catalyzed reactions. Vmax: The maximum velocity of a reaction-where it plateaus. KM: Michaelis-Constant: the [substrate] requires for 1/2 Vmax |
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Isoenzymes? |
Different enzymes that catalyze the same reactions. e.g. Glucokinase and Hexokinase |
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What are allosteric enzyme? and how do we regulate them? |
Allosteric Enzymes: prevent chaos and allow for efficient metabolism. They regulate catalytic activity. Regulation can be by inhibitors or feedback loops. It allows for immediate response to metabolic changes. |
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What are the types of Reversible Inhibitors? |
1. Competitive: compete for the active site 2. Uncompetitive: Binds to the ES complex not allowing the substrate to enter/exit the active site. 3. Non-competitive: Bind somewhere on the enzyme, altering the shape of the active site. |
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What is enzyme inhibition? |
A molecule that binds to an enzyme that decreases its activity. |
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What is the Catalytic Triad? |
A group of amino acids found in the active site that are involved in catalysis. Histidine: Generates alkoxide ion Serine: Alkoxide attacks the peptide bonds. Aspartate: Orients the histidine to accept the proton from Serine. |
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What is the structure of Heme? |
A protoporphyrin molecule with a Fe 2+ molecule in the middle. Fe makes 6 bonds. 4 to heme ring. 1 for Histidine and 1 for Oxygen. |
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Sickle Cell Anemia? |
It is a mutation in the beta unit =HbS Sickling of the RBS is the result of [high] of deoxygenated hemoglobin. It is fatal for homozygotes. |
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What does hemoglobin and Myoglobin rely on to bind to O2 |
The presence of Heme. |
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What is the basic structure of Carbohydrates? |
They are carbon based molecules rich with hydroxyls. (-OH) |
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Structure of Glucose? |
99% is in the D-Glucose ring form and 1% as an open chain. |
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What are the classes of Lipids? |
1. Free Fatty Acids: main source of fuel. 2. Triacylglycerols: storage of free fatty acids 3. Phospholipids: membrane lipids 4. Glygolipids: membrane lipids with carbohydrates 5. Steroids: most common is cholesterol |
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Key properties of Fatty Acids |
-Degree of saturation: presence of only single bonds or double bonds=kinks -Chain length: shorter=more fluid longer= less fluid |
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Types of Passive Transport? |
No energy required. 1. Simple diffusion: Fast uncontrolled movement, going down [gradient]. for small molecules: O2, CO2 N2, urea, ethanol and H2O. 2. Facilitated diffusion: Moving polar/large molecules. -Carries: Escorting the molecule across the mem. -Channels: Ion specific tunnels. e.g. Na, K, Ca. -Gates: Open by signal. Ligand or voltage. |
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Types of Active Transport? |
Energy required movement against the [gradient]. 1. Primary Active Transport: Direct use of ATP. 2. Secondary Active Transport: Uses the [gradient] to drive transport. |
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3 Types of Transport Processes |
1. Uniport: Passive transport of a single molecule (one direction) 2. Symport: Uptake of 2 substrates-flowing in the same direction 3. Antiport: Couple transport. One going in, the other going out. |
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Effects of Secondary Messengers. Most common? |
They relay the primary signal throughout the cell which results in the a physiological response. cAMP, Calcium, IP3 and DAG are the most common. |
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Phosphorylation and Dephosphorylation. |
The addition or removal of a Phosphate group. Kinase: Adds Phosphates Phosphatase: Removes phosphates |
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Products of Digestion? |
Carbs: Di and Monosaccharides. STARCH Proteins: Tri, Di and single peptides. PANCREATIC ENZYMES Lipids: free fatty acids, Glycerol (di and mono). CHYLOMICRONS. |
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Purpose of Digestion? |
Break large molecules into smaller building blocks for growth, repair and energy. Breaking down complex compounds into acetyl CoA |
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Absorption of Fat |
IT must bypass the liver because the liver easily absorbs fat and could put it in the blood. |
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3 types of carriers? |
1. Activated electron carriers for fuel oxidation: NAD+ and FAD 2. Activated electron carriers for synthesis: NADP 3. Activated 2-Carbon Carrier: CoA and acetyl CoA |
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Purpose of Glycolysis? |
Take glucose and transforming into pyruvate. |
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Key enzymes? |
The key enzyme is PFK-phosphofructokinase. |
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What is the difference between Irreversible and Reversible Regulation of Glycolysis. |
irreversible enzymes: Hexokinase, PFK and Pyruvate Kinase. Reversible enzymes:follow the flow dictated by the irreversible ones. down [gradient]. |
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Glucose Transporters? |
-Glut 1 and 3: Found in mammalian cells. Low Km, High affinity. -Glut 2: Found in liver/pancreas cells to regulate insulin. High Km, Low affinity. -Glut 4: Insulin/contraction dependent, translocating glucose to the cell surface. Moderate Km. |
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Where does Glycogenesis occur? |
It mainly occurs in the liver, and slightly in the kidneys. |
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What is the purpose of Glycogenesis and the precursors? |
The purpose is the transform pyruvate into glucose. It is the ability to make glucose from noncarbohydrate precursors. |
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Pyruvate Dehydrogenase PDH |
A complex of three enzymes that convert pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. 1. Oxidative Decarboxylation 2. Transacetylase 3. Enzyme Reoxidation |
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PDH Structure |
It is tetrameric, composed of two α- and two β- subunits. |
