3.8, 3.12, 4.1, 4.2
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
Help!
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| show | a few days
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| a _____ protein is more readily degraded than ______ protein | show 🗑
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| show | chemical or physical damage
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| show | targets protein for degradation (attachment of peptide), sends to proteasome
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| proteasome | show 🗑
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| show | any molecule that is bound to and affects a protein by either electrical attractions or weaker attractions due to hydrophobic forces
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| show | the region of a protein where a ligand binds
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| show | it changes the conformation of protein (either activates it or inhibits it)
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| show | the stronger the attraction
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| for a ligand to be able to bind to a protein.. | show 🗑
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| show | shape
structure
chemical composition
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| chemical specificity | show 🗑
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| what does chemical specificity depend on? | show 🗑
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| show | bind a number of related proteins
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| the less specific a mlx is... | show 🗑
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| show | the degree of specificity
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| show | WILL IT BIND & STAY BOUND
the STRENGTH of the ligand-protein binding
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| show | affinity
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| show | chemical specificity ; affinity
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| show | very little of the ligand is needed to bind to the protein
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| show | the fraction of total binding sites that are occupied at any given time
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| all binding sites are occupied | show 🗑
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| show | 50% saturation
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| show | 1. the concentration of unbound ligand in the solution
2. the affinity of the binding site for the ligand
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| show | the more likely it is a ligand enters a binding site and binds
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| even if specificity is low, what can drive binding? | show 🗑
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| competition | show 🗑
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| show | when a protein has two binding sites and the binding of a ligand to one of the sites alters the shape and activity of the other site
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| show | carries out the protein's physiological function
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| regulatory site | show 🗑
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| what happens to a modulator in allosteric modulation? | show 🗑
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| covalent modulation | show 🗑
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| show | adding a phosphate group to hydroxyl
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| is covalent modulation permanent or reversible? | show 🗑
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| show | enzymes
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| kinase | show 🗑
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| show | enzyme that REMOVES the phosphate group from a protein
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| the rates of enzyme-mediated runs can be increased by.. | show 🗑
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| show | when the active binding site of every enzyme is occupied by a substrate
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| what happens when the substrate concentration is too high concerning glucose in the kidney? | show 🗑
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| show | the saturation point is twice as high
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| in order to change concentration of an enzyme... | show 🗑
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| show | 1. does NOT undergo a chemical change as a consequence of the reaction that it catalyzes
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| second characteristic of enzymes | show 🗑
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| show | enzyme increases rate of chemical reaction but doesn't cause a reaction to occur that wouldn't occur in its absence
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| fourth characteristic of enzymes | show 🗑
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| show | helps binding and protein shape but does not participate in reaction
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| what type of mlx are co-factors? | show 🗑
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| show | iron
helps O2 bind
allows hemoglobin to go from oxygenated state to deoxygenated state
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| co-enzyme | show 🗑
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| what type of mlx are co-enzymes? | show 🗑
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| show | B vitamins
NAD+, binds to alcohol mlx and helps them break down
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| fat-soluble vitamins | show 🗑
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| show | movement of mlx from one location to another bc of random thermal motion
requires no energy or heat
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| show | no
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| show | oxygen, nutrients, and other mlx entering capillaries
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| show | down their concentration gradient
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| show | increase temperature
increase magnitude of difference in solute concentration from one side to another
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| show | the amount of material crossing a surface in a unit of time
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| diffusion equilibrium | show 🗑
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| show | -temp
-mass of mlx
-surface area
-medium the mlx are traveling through
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| what is the major limiting factor of membranes | show 🗑
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| show | diffuse into cells slowly or not at all
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| examples of polar molecules | show 🗑
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| show | will diffuse easily because they have large permeability coefficients
can dissolve in non polar regions of membrane occupied by the fatty acid chains of phospholipids
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| example of non-polar mlx | show 🗑
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| ion channel | show 🗑
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| ion channels have selectivity based on... | show 🗑
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| show | process of opening/ closing ion channels
can occur many times each second
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| show | binding of a ligand results in opening of the channel
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| mechanically-gated ion channels | show 🗑
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| voltage-gated ion channels | show 🗑
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| one function of membrane transport proteins | show 🗑
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| what is the charge inside of the cell? | show 🗑
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| show | no
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| where do the opposite charges align? | show 🗑
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| show | integral membrane proteins
mediate the passage of large/polar molecules
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| show | movement of substances through the membrane
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| show | solute concentration
affinity of transporters for solute
# of transporters in membrane
rate of conformational change
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| two types of mediated transport | show 🗑
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| facilitated diffusion | show 🗑
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| active transport | show 🗑
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| show | primary and secondary active transport
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| show | hydrolysis of ATP by a transport, directly relies on ATP
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| example of primary active transport | show 🗑
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| show | Na+ 15 mM
K+ 150 mM
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| show | Na+ 145 mM
K+ 5 mM
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| secondary active transport | show 🗑
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| two binding sites of transporters in secondary active | show 🗑
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| show | high to low
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| show | indirectly
uses stored energy in the ion to get the substrate into cell because it is moving against its concentration gradient
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| show | movement of actively transported solute into cell (same direction as Na+)
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| show | movement of actively transported solute OUT of cell (opposite of Na+)
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Created by:
thomask9
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