Term
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Definition
| Biological molecule that has low solubility in water and high solubility in nonpolar organic solvents |
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Term
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Definition
Long chain of carbons truncated at one end by a carboxylic acid
Maximum number of carbons in humans is 24 |
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Term
| Structure and function of triglycerides (triacylglycerols) |
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Definition
Three carbon backbone (glycerol) attached to three fatty acids
Store energy, provide thermal insulation and padding |
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Term
| Structure and function of phospholipids |
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Definition
Glycerol backbone, two fatty acids, and one polar phosphate group laying on the opposite side of the fatty acids
Phospholipids are amphipathic
Function as major component of membranes |
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Term
| Structure and function of a steroid |
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Definition
Four ringed structure
Regulate metabolic activities |
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Term
| Where does lipid synthesis and modification occur? |
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Definition
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Term
| How are lipids transported through the blood stream? |
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Definition
Lipoproteins (VLDL, LDL, HDL)
Decrease lipoprotein density by increasing ratio of lipids:protein |
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Term
| List the four major functions of lipids |
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Definition
1. Phospholipids serve as structural component of membranes
2. Triglycerides store metabolic energy and provide thermal insulation and padding
3. Steroids regulate metabolic activities
4. Some fatty acids (eicosanoids) serve as local hormones |
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Term
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Definition
| Covalent bond between carboxyl group and amino group of different molecule |
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Term
| How many alpha amino acids are there? How many are essential in humans? |
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Definition
| 20 alpha amino acids; 10 are essential (cannot be manufactured by body) |
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Term
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Definition
| An amino acid in a polypeptide chain |
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Term
| What is the amino acid "backbone"? |
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Definition
H2N -- CH -- COOH
(R group bonded to CH) |
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Term
| What are the four types of R groups in amino acids? |
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Definition
| Nonpolar, Polar, Acidic, and Basic |
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Term
| What is the only amino acid R group that can form covalent (disulfide) bonds? |
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Definition
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Term
| How many polar R groups are there, and what are they? |
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Definition
6
1. Serine
2. Threonine
3. Cysteine
4. Tyrosine
5. Asparagine
6. Glutamine |
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Term
| How many acidic R groups are there and what are they? |
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Definition
2
1. Aspartic Acid
2. Glutamic Acid |
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Term
| How many basic R groups are there and what are they? |
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Definition
3
1. Lysine
2. Arginine
3. Histidine |
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Term
| What is primary structure of proteins? |
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Definition
The number and sequence of amino acids
All amino acids have primary structure |
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Term
| What is the secondary structure of amino acids? |
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Definition
α-helix or β-pleated sheets
Most amino acids have secondary structure |
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Term
| What is tertiary structure of amino acids? |
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Definition
3D shape formed when the peptide chain curls and folds
Some larger proteins have tertiary structure |
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Term
| What is quaternary structure of proteins? |
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Definition
Two or more polypeptides bonding together
Some larger proteins have quarternary structure |
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Term
| What are the five forces that create the tertiary structure of an amino acid? |
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Definition
1. Covalent disulfide bonds between two cysteine amino acids on different parts of chain
2. Electrostatic (ionic) interactions between acidic and basic side chains
3. Hydrogen bonds
4. Van der Waals forces
5. Hydrophobic side chains pushed away from water to center of protein |
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Term
| Emprical formula of a carbohydrate? |
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Definition
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Term
| What types of carbohydrates occur most commonly? |
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Definition
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Term
| What three polysaccharides are formed from glucose? |
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Definition
Glycogen (humans)
Starch (plants)
Cellulose (plants) |
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Term
| Explain the difference between α-glucose and β-glucose. |
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Definition
In α-glucose the 1 and 6 carbon functional groups are on opposite sides of molecule, in β-glucose they are on same side.
Animals can eat α-glucose but only bacteria can digest β-glucose |
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Term
| What three parts does a nucleotide consist of? |
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Definition
1. Pentose sugar
2. Nitrogenous base
3. Phosphate group |
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Term
| How do enzymes increase reaction rates? |
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Definition
| By lowering the activation energy for the reaction; they do not effect equilibrium |
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Term
| Explain saturation kinetics |
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Definition
| As the relative concentration of substrate increases, the reaction rate increases, but only to a certain point (maximum rate: Vmax) |
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Term
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Definition
A non-protein compound that helps enzymes reach optimal activity (only required for some enzymes)
Can be coenzymes (cosubstrates and prosthetic groups) or metal ions |
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Term
| What three environmental factors affect the reaction rate of enzymes? |
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Definition
| Temperature, pH, and substrate concentration |
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Term
| Explain competitive inhibition |
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Definition
An inhibitor reversibly binds to an enzyme's active site, thus preventing the substrate from binding
Can overcome competitive inhibition by increasing substrate concentration |
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Term
| Explain noncompetitive inhibition |
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Definition
An inhibitor reversibly binds to an enzyme somewhere other than the active site, thus changing the enzyme shape/conformation and preventing substrate from binding at active site
Cannot be overcome |
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Term
| Explain irreversible inhibition |
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Definition
| Inhibitors that bind covalently to enzymes and disrupt their function |
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Term
| What is a zymogen/proenzyme? |
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Definition
| An enzyme in its inactive form (i.e. pepsinogen) |
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Term
| Explain positive cooperativity |
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Definition
| Binding by the first substrate changes the enzyme conformation/shape making it easier for other substrates to bind to the enzyme |
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Term
| What is the difference between lyase and ligase? |
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Definition
| Both catalyze addition reactions, but ligase requires energy from ATP or other molecule, lyase does not require energy |
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Term
| What is the difference between Kinase and Phosphatase? |
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Definition
Kinase phosphorylates something
Phosphatase dephosphorylates something |
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Term
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Definition
| To build or synthesize molecules |
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Term
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Definition
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Term
| Where does glycolysis occur? |
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Definition
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Term
| How many ATPs does glycolysis produce? |
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Definition
| 4 total ATPs, but 2 ATP are consumed, so it produces 2 net ATPs |
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Term
| What are the products of glycolysis? |
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Definition
2 net ATP
2 Pyruvate
2 NADH |
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Term
| How many ATPs does anaerobic respiration produce? |
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Definition
| 2 net ATPs (from glycolysis) |
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Term
| What is the purpose of of fermentation? |
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Definition
| It recycles NADH back to NAD+ for glycolysis |
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Term
| How many ATP does aerobic respiration produce? |
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Definition
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Term
| Where does the Kreb's Cycle occur? |
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Definition
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Term
| How many turns of the Kreb's Cycle does one glucose molecule produce? |
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Definition
| Two turns (one for each pyruvate formed in glycolysis) |
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Term
| What are the products of one turn of the Krebs Cycle? |
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Definition
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Term
| How many ATP does one NADH produce? |
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Definition
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Term
| How many ATP does one FADH2 produce? |
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Definition
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Term
| Where does the electron transport chain occur, and what is the final electron acceptor? |
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Definition
In the inner mitochondrial membrane
Oxygen |
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Term
| Explain the difference between oxidative phosphorylation and substrate level phosphorylation. |
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Definition
Oxidative phosphorylation occurs along the electron transport chain and uses energy released by oxidation of nutrients to produce ATP
Substrate level phosphorylation occurs during glycolysis and the Krebs Cycle. It adds a free phosphate to ADP, forming ATP. |
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Term
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Definition
| A component of many second messenger systems |
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