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88 Cards in this Set
- Front
- Back
- 3rd side (hint)
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Where are proteins (made in the cell) found? |
Embedded (integral) or attached (peripheral) to the plasma membrane Or in cell cytosol |
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Metabolism |
Combination of all chemical reactions in the body |
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Catabolic reactions |
Break down molecules to release energy |
Hydrolysis reaction (cellular respiration) |
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Anabolic reactions |
Use energy to build complex molecules from simple ones |
Condensation reaction |
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Bioenergetics |
Flow of energy in biochemical systems |
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Energy |
ATP, capacity to do work |
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Kinetic energy examples |
Muscle activity, light, thermal energy, movement |
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Potential energy example in the body |
Chemical bonds, storing nutrients (P.E.) for later |
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Thermodynamics |
How much energy are we using/releasing. Net outcome |
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What type of system is the body |
Open system (matter always being exchanged) |
Closed or open |
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Why are cells an open system |
Always obtaining nutrients (energy), processing (converting energy), and releasing waste |
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Free energy |
Quantity of usable energy (free to use) |
Delta G |
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Calculating net outcome |
Energy of product - energy of reactant |
Covalent bonds have certain amount of energy |
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Exergonic reaction |
Energy is released as reactant is converted to product Spontaneous reaction |
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Why is exergonic spontaneous |
Does not require energy for it to start |
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Endergonic reaction |
Energy is absorbed as reaction proceeds Non-spontaneous |
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Product has less energy than reactant |
Exergonic reaction |
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Product has more energy than reactant |
Endergonic Needs to add energy to system |
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Where do you break bonds? Endergonic or exergonic |
Both bc start w/ reactant, break bonds and make new ones |
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Substrate |
Reactant |
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Energy coupling |
Exergonic paired with endergonic. Energy released by exergonic drives endergonic reaction |
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ATP hydrolysis |
ATP and H2O makes ADP and phosphate Exergonic |
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Thermodynamics refers to |
Free energy, delG. Quantity |
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Kinetics refers to |
Rate of the reaction. Speed |
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How do you speed up a reaction |
Enzymes |
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Maltase |
Enzyme. Breaks down glycosidic linkage. Helps in breakdown of maltose (disaccharide) to glucose |
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How do enzymes speed up reaction |
Orients molecules in a way that they will find or break bonds faster |
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Activation energy is lowered by |
Enzymes |
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DelG determines |
Direction of a reaction not its rate |
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Can activation energy be abolished? |
No |
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Enzymes are related more to KE or PE |
Kinetic |
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Enzymes are made of |
Sequence of amino acids (Proteins) |
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Properties of enzymes |
-Made of proteins -does not change outcome (no interfering with thermodynamics) -interferes with kinetics -enzyme substances can be recycled |
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Do enzymes die? |
All proteins will eventually have wear and tear, denature, and break down |
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Active site |
Area on an enzyme that binds a substrate |
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Enzymes are made of |
Sequence of amino acids |
Enzymes are proteins |
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Theory of how an enzyme binds a substrate |
Induced fit theory |
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Induced fit theory |
Substrate binds to enzyme in active site and enzyme changes conformation to accommodate substrate |
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Fit of a substrate to enzyme is highly specific based on |
Shape, H-bonds, hydrophobic interactions |
3 specificities |
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Optimal conditions of enzymes |
Most want slightly basic pH, body temp (96-104.9), concentration |
Same as proteins |
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Ways of inhibiting enzymes |
Natural and artificial, genetic Competitive and non competitive |
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Why inhibit enzymes? |
Regulation, maintain homeostasis |
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Competitive inhibition |
Substrate and inhibitor compete for active site (have similar structure) |
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Property of a competitive inhibitor |
Similar structure to substrate Usually artificial inhibition |
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Competitive inhibition is dependent on |
Concentration of the substrate vs inhibitor (higher concentration wins) |
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Non-competitive inhibition Natural or artificial? |
Interacts with a different region of enzyme (not active site) Natural process |
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Property of noncompetitive inhibitor |
Always wins because when inhibitor binds, active site becomes unavailable |
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Allosteric |
Natural process (inhibitor is binding to a different region) |
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Artificial regulation of proteins |
Food or meds |
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Genetic effects on proteins |
Synthesis Proteins are made from DNA gene sequence, if gene is mutated, makes incorrect protein and loses a function |
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Anemia |
Inadequate delivery of oxygen |
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Sickle cell anemia |
Sickle cells are not flexible. Pointy so they get stuck in blood vessels One subunit of hemoglobin not functioning correctly Genetic disease |
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Messed up subunit in sickle cell anemia |
Glutamic acid (normally - charge) substituted by valine (neutral). Structure of protein in 3D depends on R group interaction. Charge change completely changes shape of protein. Instead of loose hemoglobin, form long fibers Since it's only protein in blood cells, affects entire shape |
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Hemoglobin in sickle cell anemia |
Not loose, forms long fibers (remains attached to each other) |
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How much hemoglobin in one erythrocyte? |
200 mill |
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Erythrocyte |
Red blood cell, completely made of loose hemoglobin |
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FH |
Genetic disease Liver cells have little or no LDL receptor (protein) Cholesterol builds up in blood, atherosclerosis |
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LDL |
Low-Density lipoprotein |
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PKU |
Phenylketonuria, disease caused by mutation in the enzyme, phenylalanine hydroxylase (converts phenylalanine to tyrosine) |
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Purpose of phenylalanine hydroxylase |
Converts phenylalanine to tyrosine |
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Autosomal recessive disease |
PKU |
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Tyrosine |
Precursor for neurotransmitters |
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Consequences of PKU |
Mental deterioration especially in neurons not functioning properly |
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Neuromuscular junction |
Where neurons communicate with muscles |
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Presynaptic neuron |
Communicates with neurotransmitters via electrical activities |
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Post synaptic neuron |
receives info from presynaptic neuron |
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Neurotransmitters are released into |
Synaptic cleft |
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Cocaine |
Stimulant and appetite suppressant Dopamine reuptake inhibitor Dopamine !!!transporter!!! protein blocker (DAT) |
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Cocaine vs coffee |
Dopamine transporter, adenosine receptor |
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How do neurons control muscles? |
Ach by exocytisis Acts on muscle receptors (ligand gated channels |
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Depression caused by |
decrease in serotonin |
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Fluoxetine |
Works on reuptake mechanism Ssri Effect duration in cleft by inhibiting proteins |
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How to breakdown neurotransmitters in neuromuscular junction |
ACh estrase |
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Why Block ACh receptor? |
Muscles won't respond. Good for surgeons, etc |
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Curare |
Natural way to block ACh receptors Old days |
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Old days muscle relaxant |
Curare |
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Anesthesia awareness |
Not enough pain suppressant and not enough pain suppressant |
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Neurotransmitter release is just as important as |
Neurotransmitter clearing |
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What happens if you inhibit ACh estrase |
Muscles over activated, can't relax, very tired If lungs get tired, can't breath |
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Over excitement of muscles leads to |
Fatigue ( activated too long ) |
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Clearing neurotransmitters |
1. Breakdown of neurotransmitter in synaptic cleft (degrading enzyme) 2. Reuptaking, recycling it back into presynaptic neuron |
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Chronic depression is referred to as |
Chemical imbalance |
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Serotonin caused by |
decrease in serotonin |
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Fluoxetine |
Works on reputable mechanism Ssri Effect duration in cleft by inhibiting proteins |
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Phenelzine (Nardil) |
For clinical depression MAO (monoaminooxidase) inhibitor Works on degrading protein (rather than reuptake) |
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Depression treatment |
Phenelzine (Nardil) and fluoxetine |
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Caffeine |
Stimulant Adenosine !receptor! antagonist (blocker) -increase dopamine activity |
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Function of adenosine receptor |
Regulates quantity of dopamine |
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