3.8, 3.12, 4.1, 4.2
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typical life of a protein | show 🗑
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show | degraded ; intact
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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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binding site | show 🗑
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what does the binding of a ligand do to a protein? | show 🗑
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show | the stronger the attraction
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show | it has to be close to the protein
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what is a ligand's binding ability based on? | show 🗑
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show | CAN IT BIND
allows protein to identify one particular ligand
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show | the shape of binding site
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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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what determines the side effects of drugs? | show 🗑
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show | WILL IT BIND & STAY BOUND
the STRENGTH of the ligand-protein binding
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what determines how likely it is that a bound ligand will leave the protein surface and return to its unbound state? | show 🗑
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show | chemical specificity ; affinity
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when there is high affinity... | show 🗑
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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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half the binding sites are occupied | show 🗑
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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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the greater the ligand concentration... | show 🗑
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even if specificity is low, what can drive binding? | show 🗑
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show | when more than one type of ligand can potentially bind to a certain binding site
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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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show | covalent bonding of charged chemical groups to a protein
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most common type of covalent modulation | show 🗑
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is covalent modulation permanent or reversible? | show 🗑
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show | enzymes
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show | enzyme that ADDS the phosphate group to a protein
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phosphatase | show 🗑
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show | increasing temp
increasing substrate concentration
increasing enzyme activity
increasing enzyme concentration
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show | when the active binding site of every enzyme is occupied by a substrate
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show | when glucose is too high, it will end up in urine, because the kidneys could not reabsorb
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if there is twice as much enzymes.. | show 🗑
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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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example of co-factor | show 🗑
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co-enzyme | show 🗑
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show | ORGANIC MLX (have carbons as part of their structure)
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example of co-enzyme | show 🗑
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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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does simple diffusion require ATP? | show 🗑
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show | oxygen, nutrients, and other mlx entering capillaries
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which way do mlx move in simple diffusion | show 🗑
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diffusion will speed up as... | show 🗑
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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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magnitude of flux depends on | show 🗑
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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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show | - channel diameter
- charged surface of subunits
- # of water mlx associated with ions
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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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show | open in response to physical deformation (like pressure) of receptor
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voltage-gated ion channels | show 🗑
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show | maintaining membrane potential and electrochemical gradient
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what is the charge inside of the cell? | show 🗑
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is the cell chemically balanced? | show 🗑
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where do the opposite charges align? | show 🗑
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transporters | show 🗑
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mediated transport | show 🗑
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show | solute concentration
affinity of transporters for solute
# of transporters in membrane
rate of conformational change
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show | facilitated diffusion and active transport
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show | net flux of a molecule across a membrane always proceeds from HIGH to LOW concentration
*uses a transporter to move solute
contributes significantly to metabolic homeostasis
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active transport | show 🗑
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show | primary and secondary active transport
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primary active transport | show 🗑
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show | Na+ / K+ ATPase pump
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show | Na+ 15 mM
K+ 150 mM
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concentration of Na/K+ OUTSIDE cell | show 🗑
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secondary active transport | show 🗑
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show | one for ion (normally Na+)
another for second substrate (ex: amino acid, vitamin)
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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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