Lecture 21 Flashcards

(29 cards)

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?

21
Q

Phosphorylation of eIF2 results in what?

22
Q

Phosphorylation of eIF4E results in what?

23
Q

Phosphorylation of 4E-BP results in what?

24
Q

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

A

SeCys and UGA

25
What is vitamin K used for?
- required for blood clotting | - mediates gamma-carboxylation
26
What is the use of HbA 1c?
It is a variant of HbA that gets glycosylated and can be a measurement of blood sugar level in diabetes
27
What should blood sugar levels be at?
4 - 6% Anything over 7% is too much
28
What does HbA -1c have to do with diabetes complications?
All proteins are glycated so the glycation of HbA-1c is a sample of the glycation levels of the other proteins
29
How can you have low HbA-1c levels but high blood glucose levels?
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)