Lecture 21 Flashcards

1
Q

What two places are are proteins typically made?

A

1) cytosol on free ribosomes

2) inner cytoplasmic surface of the endoplasmic reticulum (lumen which is geographically outside of the cell)

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2
Q

What happens when the protein being translated is 70 amino acids long?

A

It protrudes from the ribosome and a ribonucleo protein particle recognizes the 15 - 20 hydrophobic amino acid sequence at the proteins N terminal and binds to it, ceasing elongation.

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3
Q

How do proteins make it known that they are destined for the lysosome?

A

There will be a mannose-6-phosphate residue attached to it enzymatically

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4
Q

What occurs in I-cell disease?

A

A genetic defect in adding mannose-6-phosphate to enzymes so signaling certain proteins to go to the lysosome is impaired.

due to inclusion bodies

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5
Q

Where are nuclear proteins made, what is their signaling, and what recognizes this signal?

A
  • Free ribosomes
  • basic amino acids
  • importing and Ran proteins
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6
Q

How are proteins destined for the peroxisome targeted and who recognizes the targeting signal?

A
  • they’re given a peroxisomal targeting sequence that is recognized by PTS receptors
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7
Q

What happens in Zellweger syndrome?

A

A defect in the peroxisomal targeting of proteins

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8
Q

Why is it important to remove sulfates from molecules and what is responsible for this?

A
  • if not, consequence is progressive paralysis, skeletal deformities, and neurological defects.
  • enzymes called sulfatases
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9
Q

what is multiple sulfates deficiency?

A

genetic disease with unmodified sulfatases

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10
Q

What is Keshan disease?

A

Disease where selenium is deficient, characterized by dilated cardiomyopathy striated muscle degeneration, and a flabby heart lol
- selenium is an essential micronutrient

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11
Q

What does glutathione peroxidase do and how?

A

Reduces peroxides by converting toxic R-OOH groups back to R-OH groups

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12
Q

What is the popular reducing agent used by glutathione peroxidase?

A

glutathione

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13
Q

What converts T4 to active T3?

A

5’-deiodinase

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14
Q

What does the K in vitamin K stand for?

A

coagulation

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15
Q

What does Warfarin (Coumadin) do?

A

Inhibitor that competes with vitamin K and reduces synthesis of clotting factors 2, 7, 9, 10

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16
Q

What is the signal for Mitochondrial targeting?

A

A-terminal leader 20-80 charged AA’s

17
Q

Which amino acids do not have a Modification?

A

Gly, Ala, val, ile,leu

18
Q

what is the Mechanism of a perm?

A

reduce the sulfide bonds, then oxidize the bonds back.

19
Q

What are the sites that are usually phosphorylated?

A

ser, thr, tyr

20
Q

phosphorylation of eIF2 results in what?

A

inhibition

21
Q

Phosphorylation of eIF2 results in what?

A

inhibition

22
Q

Phosphorylation of eIF4E results in what?

A

stimulation

23
Q

Phosphorylation of 4E-BP results in what?

A

stimulation

24
Q

What is the 21st amihe acid and. what is it’s codon?

A

SeCys and UGA

25
Q

What is vitamin K used for?

A
  • required for blood clotting

- mediates gamma-carboxylation

26
Q

What is the use of HbA 1c?

A

It is a variant of HbA that gets glycosylated and can be a measurement of blood sugar level in diabetes

27
Q

What should blood sugar levels be at?

A

4 - 6%

Anything over 7% is too much

28
Q

What does HbA -1c have to do with diabetes complications?

A

All proteins are glycated so the glycation of HbA-1c is a sample of the glycation levels of the other proteins

29
Q

How can you have low HbA-1c levels but high blood glucose levels?

A

If the hemoglobin is somehow messed up and the turnover rate is high, they will be less glycated (how the fuck do you spell this word)