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what does ramphanomycin do |
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Definition
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what antibiotics stop translation |
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Definition
streptomyocin, arythromycin, tetracycline, chloramphenicol |
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what type of antibiotic is streptomyocin |
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Definition
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what type of antibiotic is arythryomicin |
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inactivate eukaryotic elongation factor 3 (eEF-2) preventing translocation |
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inactivate eukaryotic elongation factor 3 (eEF-2) preventing translocation |
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what toxins come from different sources but both inactivate eukaryotic elongation factor 3 (eEF-2) preventing translocation |
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Definition
dyptheria and pseudomonas |
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what does chloramphenicol do |
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Definition
interfere with mitochondrial protein synthesis |
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Definition
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what happens if you give too much antibiotic |
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Definition
it can inhibit mitochondrial translation |
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what happens if you give too little antibiotic |
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Definition
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how is a protein directed to a specific organell |
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Definition
it has a specific sequences |
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how does a protein ment to get translated in the RER vs the cytoplasm get to its destination |
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Definition
proteins destined for the RER begin translation in the cytoplasm but when the special sequence is found they are released and sent to the RER |
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what receptors signal for a protein to be sent to the RER |
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Definition
SRP interacts with a SRP receptor and hydrophpbic signal on the protein |
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what is the fate of the signal sequence that gets a protein to the RER for translation |
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Definition
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cleaving of a signaling sequence off a protein (EX: RER destined proteins) |
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what are some functions of trimming |
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Definition
may activate proteins when the reach their final destination so they don't mess up the cell |
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what is the function of a chaperone |
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Definition
assist proteins in folding correctly |
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what is the function of a protoelytic enzyme |
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Definition
allows proteins to remain inactive until they reach their target destination |
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what are some examples of proteins that need trimming |
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Definition
insulin, collagen, anything with a signaling sequence to go to an organell |
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what are some post translation covalent modifications |
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Definition
phosphorlyation (kinases), dephosphorlyation (phosphatases), glycosylation, hydroxylation, vitamin k dependent carboxylation, attachment of farnesyl, acetlyation |
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where do covalent post translational modifications do their work |
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Definition
on hydroxyl groups of serine, threonine, and occasionally tyrosine |
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what is the function of covalent post translational modifications |
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addition of sugar residues to proteins |
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what types of ways can glycosylation occur |
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Definition
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what participates in an n link |
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Definition
amide nigtogen of asparagine participating in glycosylation |
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what participates in an o link |
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Definition
serine or threonine hydroxyl participating in glycosylation |
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what proteins is glycosylation associated with |
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Definition
membrane proteins, lysosomal proteins, secreted proteins |
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give an example of hydroxylation |
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Definition
proline and lysing in collagen, important in cross linking fibers |
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how does vitamin k modify proteins |
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Definition
it carboxylates glutamate residues required for blood clotting |
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what is the purpose of attaching a farnesyl group (lipid) to a protein |
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Definition
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give an example of acetylation |
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Definition
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what is the function of acetylation |
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Definition
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describe the synthesis of insulin |
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Definition
1. initially there is a long precursor protein 2. it is targeted to the RER 3. the signal is removed 4. disulfide bonds are made to join end fragments 5. c-peptide between fragments is cleaved 6. c-peptide and insulin are stored in secretory granules |
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why can c-peptide be used to measure insulin levels |
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Definition
it is send into the blood with insulin but lasts 30 min vs 5 min so it is always at a higher concentration |
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why do we think that c-peptide has no function |
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Definition
it isnt in artificial insulin and those people are fine |
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why is c-peptide useful when people are using artificial insulin |
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Definition
if they go into diabetic shock, you can measure c-peptide to tell if it was because of the medication or their own insulin production |
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describe the synthesis of collagen |
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Definition
1. translated in RER 2. hydroxylated 3. glycosylation 4. disulfide bond formation resulting in triple helix 5. ends cleaved off 7. triple helix is cross linked |
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what disease does a vitamin C deficiency cause |
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Definition
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how does vitamin deficiency cause disease |
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Definition
it is a cofactor for hydroxylation of proline and lysine in collagen |
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what are the symptoms of scurvy |
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Definition
bruise easily, loose teeth, bleeding gums, poor bone development, poor wound healing |
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where does the disulfide bond formation in insulin processing occur |
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Definition
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where does the clevage of c-peptide in insulin processing occur |
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Definition
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what does a mutation in the collagen gene causing buliker amino acids to replace glycine cause |
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what are the symptoms of type 1 osteogenesis imperfecta |
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Definition
less erver, suspect of child abuse |
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what are the symptoms of type 2 osteogenesis imferfecta |
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Definition
fatal in utero or nenonatal period |
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what are the symptoms of osteogenesis imperfects |
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Definition
brittle bones, blue slera of eyes, hearing loss, dental imperfections |
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what causes ehlers-alantos syndrome |
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Definition
EDS multiple mutations in the collagen genes or collagen enzymes (collagen pepsidase) |
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what are the symptoms of ehlers-alantos syndrome |
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Definition
hyperextensiable skin, hypermobile joines, easy bleeding or bruising, potentially lethal vascular problems due to collagen in arteries |
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what causes menkes disease |
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Definition
mutation in copper transport protein leading to a copper deficiency. lysol oxidase cross links collagen fibrils and needs coper to do it |
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what are the symptoms of menkens disease |
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Definition
kinky hair, steely hair color, adrenal rupture, cerebral degeneration (retardation), osteoperosis, anemia |
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how does the cell know proteins are suposed to go to the lysosome |
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Definition
there is a a phosphorylation at a specific manos |
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what is the word that describes the functional role of the lysosome |
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Definition
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Definition
extracellular proteins and membrane surface proteins, intracellular proteins that are damaged or need turnover, proteins tagged by ubiquitin |
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what causes i-cell disease |
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Definition
proteins that are suposed to go to the lysosome are not phosphorylated so they are sent outside the cell and the lysosome cannot digest and they become engourged. the cells that got let out degrade the body |
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