Term
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Definition
| A carbon that has 4 different attachment groups |
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Term
| How do you tell a D sugar from an L sugar |
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Definition
D sugar - the chiral carbon farthest from the aldehyde has an -OH group on the RIGHT
L sugar - the chiral carbon farthest from the aldehyde has an -OH group on the LEFT |
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Term
| What causes a phospholipid to spontaneously orient itself into a membrane bilayer? |
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Definition
| The nonpolar part is exceluded from the aqueous environment because it cannot form H-bonds |
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Term
| Which lipoprotein is often engulfed by foam cells to initiate a plaque? |
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Definition
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Term
| Which lipoprotein is the primary transporter of dietary fats from intestinal cells |
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Definition
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Term
| Which lipoprotein contains primarily triglycerides and Apo B-48? |
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Definition
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Term
| Which lipoprotein is the primary fraction in the exogenous pathway? |
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Definition
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Term
| Which protein transports free fatty acids from fat cells to muscle cells? |
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Definition
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Term
| Which lipoprotein is the "scavenger" that picks up excess cholesterol |
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Definition
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Term
| Which lipoprotein originally contains Apo A, Cii, and E? |
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Definition
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Term
| Which lipoprotein is the primary carrier of dietary carbs that have been converted to fats? |
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Definition
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Term
| Which lipoprotein fraction contains primarily TG's and APpo B-100? |
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Definition
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Term
| Which pathway or process involves cholesterol being returned to tissues by chylomicrons? |
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Definition
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Term
| Which pathway or process involves distribution of triglycerides from dietary fats? |
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Definition
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Term
| Which pathway or process involves the distribution of triglycerides from dietary carbs? |
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Definition
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Term
| Which pathway or process returns cholesterol to the liver primarily by LDL's? |
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Definition
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Term
| Which pathway or process involves removal of excess cholesterol from tissues by HDLs? |
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Definition
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Term
| Where are HDL's synthesized? |
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Definition
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Term
| Which apoproteins do HDL's contain? |
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Definition
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Term
| What apoprotein(s) do LDL's start out with? |
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Definition
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Term
| Where is LDL synthesized? |
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Definition
| It isn't. It is leftover remnants of chylomicrons and VLDLs |
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Term
| Which apoprotein(s) do chylomicrons start out with? |
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Definition
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Term
| where are chylomicrons synthesized? |
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Definition
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Term
| where are VLDL's synthesized? |
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Definition
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Term
| Which Apo proteins do VLDL's have? |
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Definition
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Term
| What carries most cholesterol back to the liver? |
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Definition
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Term
| Why are HDLs considered "good cholesterol" and LDL's considered "bad cholesterol"? |
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Definition
| LDL's can get oxidized, which cause them to be engulfed by macrophages to form foam cells, and get sequestered as plauqes. HDL's can scavenge the sequestered cholesterol and get it back to the liver for removal. |
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Term
| What two metabolic reactions are coupled to the production of an NADH? |
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Definition
Oxidation of an alcohol to an aldehyde (or ketone)
and Oxidation of a C=O to a -COOH |
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Term
| What metabolic reaction is coupled to the production of FADH2? |
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Definition
| Oxidation of a C-C to a C=C |
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Term
| Which complex in the ETC receives electrons from FADH2? |
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Definition
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Term
| Which complex in the ETC receives electrons from CoQ? |
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Definition
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Term
| Which complex in the ETC receives electrons from NADH? |
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Definition
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Term
| Which complex in the ETC passes electrons to oxygen? |
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Definition
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Term
| Which complex in the ETC passes electrons to CoQ? |
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Definition
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Term
| Which complexes in the ETC pump protons across the inner membrane? |
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Definition
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Term
| Describe how bacteriorhodopsin was used to support the chemi-osmotic theory. |
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Definition
| bacteriorhodopsin is a proton pump, and when an artificial vesicle was created with it + ATP synthase, the ATP synthase was functional and produced ATP. |
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Term
| How does the DNP molecule help us understand the proton motoive force and chemi-osmotic theory? |
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Definition
| DNP is an uncoupling protein that can shuttle protons across the inner mitochondrial membrane without production of ATP ( when DNP is present, atp synthesis is decreased) |
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Term
| Describe how activation of the uncoupler protein helps an infant stay warm. |
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Definition
| When an uncoupler protein shuttles protons across the inner membrane, energy is not consumed in ATP synthesis. instead, heat is generate to keep the baby warm. |
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Term
| What hormone would be most prominent during fasting? |
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Definition
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Term
| Shortly after a big meal, hormone sensitve lipase is turned off by dephosphorylation. what hormone is responsible for controlling the dephosphorylation? |
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Definition
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Term
| What role does hormone sensitive lipase play during fasts? |
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Definition
| HSL tells fat cells to hydrolizes triglycerides into glycerol and free fatty acids for use by the rest of the body |
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Term
| At the end of an overnight fast, how active are GLUT transporters in the brain? |
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Definition
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Term
| At the end of an overnight fast, how active are GLUT transporters in the red blood cells? |
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Definition
| very active or moderately active |
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Term
| At the end of an overnight fast, how active are GLUT transporters in the liver cells? |
|
Definition
| moderate to slow activity |
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Term
| At the end of an overnight fast, how active are GLUT transporters in the fat cells? |
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Definition
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|
Term
| At the end of an overnight fast, how active are GLUT transporters in the muscles? |
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Definition
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Term
| At the end of an overnight fast, how active are LPL's near muscle cells? |
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Definition
| very active to moderately active |
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Term
| At the end of an overnight fast, how active are LPL's near fat cells? |
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Definition
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Term
| At the end of an overnight fast, how active are LPL's near liver cells? |
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Definition
| moderately active to slow |
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|
Term
| At the end of an overnight fast, how active are transporters in the kidneys? |
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Definition
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Term
| At the end of an overnight fast, how active are transporters in the intestines? |
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Definition
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Term
| At the end of an overnight fast, how active are fatty acid synthesis enzymes? |
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Definition
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Term
| At the end of an overnight fast, how active is hormone sensitive lipase in fat cells? |
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Definition
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|
Term
| What transport systems use active transport? |
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Definition
| only the intestines and kidneys |
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|
Term
| What transport systems are insulin dependent? |
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Definition
| GLUT 4's transporter in the muscle and fat cells |
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Term
| What are the relevant properties of the amino acid aspartate ASP? |
|
Definition
| negative, acidic, charged, polar |
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Term
| What are the relevant properties of the amino acid glutamate GLU? |
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Definition
| negative, acidic, charged, polar |
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Term
| What are the relevant properties of the amino acid arginine ARG? |
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Definition
| positive, basic, charged, polar |
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Term
| What are the relevant properties of the amino acid lysine LYS? |
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Definition
| positive, basic, charged, polar |
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Term
| What are the relevant properties of the amino acid histidine HIS? |
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Definition
| charged, positive, basic, polar, PKA IS 6, so at PH of 7.4, it has no charge. |
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Term
| What are the relevant properties of the amino acid serine SER? |
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Definition
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Term
| What are the relevant properties of the amino acid tyrosine TYR? |
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Definition
| uncharged, polar, aromatic |
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Term
| What are the relevant properties of the amino acid alanine ALA? |
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Definition
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|
Term
| What are the relevant properties of the amino acid glycine GLY? |
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Definition
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Term
| What are the relevant properties of the amino acid methionine MET? |
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Definition
| nonpolar, sulfur containing, methyl donor |
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Term
| What are the relevant properties of the amino acid cysteine CYS? |
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Definition
| nonpolar, sulfur containing, forms disulfide bonds |
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Term
| What are the relevant properties of the amino acid phenylalanine PHE? |
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Definition
| nonpolar, aromatic, VERY hydrophobic |
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Term
| What are the relevant properties of the amino acid valine VAL? |
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Definition
| nonpolar, aliphatic, very hydrophobic |
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Term
| What are the relevant properties of the amino acid leucine LEU? |
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Definition
| nonpolar, aliphatic, very hydrophobic |
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Term
| What are the relevant properties of the amino acid isoleucine ILE? |
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Definition
| nonpolar aliphatic, very hydrophobic |
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Term
| When pH equals the pKa for an ionizable group, what can be said about the charged and uncharged species? |
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Definition
| equal amounts of charged and uncharged species exist, resulting in a 1/2 charge |
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Term
| what affect does a mutation such as sickle cell (Glu-->Val) have on the function of HbS vs HbA |
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Definition
| Sickle cell Hgb exposes valine (a hydrophobic) to the outer surface of the protein, causing confromational changes that allow the Hgb to polymerize when it is deoxygenated. |
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Term
| What types of bonding is representative of primary protein structure? |
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Definition
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|
Term
| what is primary protein structure? |
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Definition
|
|
Term
| what is secondary protein structure? |
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Definition
| it is hydrogen bonding between peptide bond atoms on the polypeptide, resulting in alpha helices and beta pleated sheets. |
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Term
| What is tertiary protein structure? |
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Definition
| it minimizes volume and hides the hydrophobics. things fold to maximize H-bonds between side chains, and sometimes we get S-S bonds to lock it in place. |
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Term
| What is quaternary protein structure? |
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Definition
| involves at least 2 different peptide chains, they combine in order to minimize hydrophobics and maximize H-bonds |
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Term
| A left shift in the hemoglobin curve causes what changed in binding affinity? |
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Definition
| it increases binding affinity |
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Term
| A right shift in the hemoglobin curve causes what changed in % O2 saturation? |
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Definition
| His hemoglobin would want to unload, so his O2 saturation would decrease. |
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Term
| What four factors cause Hgb curve to have a left shift? (think lungs) |
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Definition
| decreased CO2, decreased BPG, decrease in hydrogen ion concentration (increase pH), and a decrease in temperature |
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Term
| what four factors cause Hgb curve to have a right shift? (think capillaries) |
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Definition
| increased temperature, increased BPG, increased CO2, increased hydrogen ion concentration (decrease in pH) |
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Term
| With conditions in the capillary beds, does Hgb's oxygen affinity increase or decrease? explain |
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Definition
| Hgb's O2 affinity would decrease, because we want to release our O2 in the capillary bed, so binding affinity decreases, allowing O2 to pop off |
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Term
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Definition
| The Bohr effect says that hemoglobin binding affinity is inversely related to both CO2 concentration and [H+] concentration. As CO2 decreases, affinity increases. As[H+] increase (ph decrease) binding affinity decreases |
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Term
| What are the relevant properties of the amino acid proline PRO? |
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Definition
| nonpolar, aliphatic, cyclic, uncharged |
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Term
| What are the relevant properties of the amino acid tryptophan TRP? |
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Definition
| nonpolar, aromatic, uncharged |
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|
Term
| What are the relevant properties of the amino acid asparagine ASN? |
|
Definition
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|
Term
| What are the relevant properties of the amino acid glutamine GLN? |
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Definition
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|
Term
| What are the relevant properties of the amino acid threonine THR? |
|
Definition
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Term
| What reactions do hexokinase and glucokinase carry out, and what is their physiological significance? |
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Definition
| Both phosphorylate glucose, however hexokinase has a very low Km (high affinity) because it is active in muscles during fasts. Glucokinse has a higher Km (lower affinity) because it is only active in the liver when glucose levels are high after a meal. |
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Term
| Why do the liver, kidney and intestinal cells not “want” to phosphorylate glucose they have inside their cells? |
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Definition
| Because these cells are want to export glucose to the rest of the body, and phosphorylating it would keep it in the cells. |
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Term
| How does ATP affect phosphofructokinase (PFK) activity? |
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Definition
| When ATP is high, we don't need a lot of energy, so ATP inhibits PFK by increasing Km, decreasing affinity |
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Term
| How does AMP affect phosphofructokinase (PFK) activity? |
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Definition
| When AMP is high, we need more energy, so AMP will activate PFK by decreasing Km, increasing affinity. |
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Term
| What does phosphofructokinase do? |
|
Definition
| it phosphorylates fructose-6-p in glycolysis (1st committed step) |
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|
Term
| Which paramenter, Km or Vmax, is affected by allosteric inhibitors (or activators)? |
|
Definition
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|
Term
| What does an allosteric inhibitor do? |
|
Definition
| it binds to the enzyme at somewhere other than the active site, resulting in a change in conformation that increases Km, decreases affinity. |
|
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Term
| what does an allosteric activator do? |
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Definition
| it binds to the enzyme and somewhere other than the active site, resulting in a change in conformation that decreases Km, increases affinity. |
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