Term
Folding starts-- but it is not neccessarily the -- structure
folding is complete- |
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Definition
immediately on the ribosome
final/correct structure
after peptide leaves ribosome |
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Term
Proteins are synthesized as a --dimensional sequence
without regard to --dimensional final structure |
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Definition
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Term
| If a Protein folds correctly by itself it makes a: |
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Definition
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Term
| If a protein doesn't fold correctly by itself it - |
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Definition
| can fold correctly with a chaperone protein which leads to a functional protein. |
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Term
| If a protein (with or without a chaperone) folds incorrectly either- or - |
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Definition
| leads to aggregation or degraded proteasomes. |
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Term
| Heat shock proteins are expressed in response to -- because -- therefore chaperones-- |
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Definition
elevated temperature or cell stress.
b/c protein folding is affected by heat. Therefore chaperones can repair potential damage of misfolding |
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Term
| How many chaperones in all cells? |
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Definition
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Term
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Definition
| help with protein folding/ or just help bloack aggregation. |
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Term
| Unfolded/misfolded proteins may form |
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Definition
| large, insoluble conglomerates in cells |
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Term
| protein aggregation sometimes happens when -- |
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Definition
| when overexpressing eukaryotic proteins in bacteria |
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Term
| protein aggregation diseases: |
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Definition
• Huntington’s disease
• Alzheimer’s disease•
Prion diseases-
• Creutzfeldt-Jacob disease
• Chronic wasting disease
• Mad cow disease |
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Term
| Misfolded proteins can alter the conformation of -- by -- |
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Definition
other proteins:
Formation of disease- causing amyloid fibrils |
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Term
| most proteins are -- after tranlation in the --. Proteolysis= |
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Definition
covalently modified, golgi apparatus.
cleaving of protein leading to activation (insulin) or degredation |
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Term
| where is Processing pathway for insulin |
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Definition
| Beta cells of the islets of Langerhans in the pancreas |
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Term
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Definition
| "network inside the part of a cell that is outside the nucleus" |
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Term
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Definition
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Term
| ER with ribosomes attached |
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Definition
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Term
| ER with no ribosomes attached = |
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Definition
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Term
| processing pathway for insulin- |
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Definition
1. mRNA codes for preproinsulin on cystosolic ribosomes on the rough ER
2. peptide transported into lumen of ER.
3. signal seq. at the N-terminal end of preproinsulin is removed (proteolysis) to form proinsulin
4. proinsulin is stored in ER lumen until signal releases it.
5. signal arrives and proinsulin-> insulin as it passes thru golgi to blood. |
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Term
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Definition
2 biologically active
insulin +C peptide |
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Term
| Insulin structure has -- that have to be between those specific -- to be --. If between others it will be -- |
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Definition
three disulfide bonds
cystienes if to be active
inactive |
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Term
| Preproinsulin squirms from --to -- the signal seq is removed by -- the peptide bond between --and the -- is cleaved. |
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Definition
ribosomes to lumen of ER
proteolitic action/ enzymes
C terminal of the signal seq
N terminal of the B seq |
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Term
The proinsulin =
folds
major reason for- |
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Definition
| the molecule that enters the lumen of the ER folds such that disulfide bonds are made between proper cystadine groups which is major reason it is a precursor to insulin. |
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Term
| How does the proinsulin fold? |
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Definition
| The 3 pairs of cystadines become adjacent to each other to make proper disulfide bonds |
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Term
| -- direct aa translocation into the ER. |
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Definition
| Amino-terminal signal sequences |
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Term
| AA terminal signal seq description |
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Definition
| Lys or Arg comes before a hydrophobic core. Right before a cleavage site is a Gly or Ala (polar short side chain) |
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Term
ribosome starts making a polypetide at the --' end at the start seq=
the first 20 aa are- recognized by-- |
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Definition
5' GUA
signal seq
sgnal requenition particle (SRP) which opens a channel. |
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Term
| how are EUK proteins directed to ER lumen? |
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Definition
| mRNA and ribsome at start codon make the first part of signal seq wich the SRP binds to. SRP then is recognized by receptor on ER which forms a channel and lets the chain enter the ER. |
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Term
| Proteins are moved from the ER to the -- in transport vesicles. Sorting occurs primarily in the -- |
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Definition
cis side of the Golgi complex
trans side of the Golgi complex. |
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Term
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Definition
1. dnaJ binds to unfolded protein and then the DNA K.
2. DNA J stimulates the atp hydrolysis of dnaK. dnak-atp complex binds tight to protein
3. GrPE stimulates the release of ADP
4. ATP binds to dnaK again and the protein dissociates
5. protein is either folded correctly or it repeats the cycle or it goes to GroEL cycle |
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Term
| protein enters - golgi and exits- |
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Definition
enters on cis side
exits on trans |
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Term
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Definition
| specific adenine from the 28S rRNA and disrupts protein synthesis. |
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