Post Translation Modification of Proteins Flashcards

1
Q

what does post translation modification do?

A

converts inactive proteins to active

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2
Q

trimming

A

removing part of polypeptide chain for activation

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3
Q

enzyme that trims large precursor molecules

A

endoproteases

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4
Q

intracellular trimming ex

A

insulin:

preproinsulin -> proinsulin -> insulin

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5
Q

extracellular trimming ex

A

zymogens are activated after they reach site of activation

pepsinogen -> pepsin in stomach
trypsinogen -> trypsin in intestine

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6
Q

covalent modification of amino acids can be modified to achieve:

A
  1. alter activity or stability of protein
    2, direct protein to cellular compartment
  2. prepare protein for secretion from cell
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7
Q

where do covalent modifications take place?

A

in endoplasmic reticulum and golgi apparatus

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8
Q

covalent modifications include:

A
  1. phosphorylation
  2. glycosylation
  3. acetylation or methylation
  4. hydroxylation
  5. carboxylation
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9
Q

phosphorylation mechanism

A

addition of phosphate(phosphorylation) by kinase or removal by phosphatase (dephosphorylation)

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10
Q

glycosylation

A

addition of carb to protein forming glycoprotein or proteoglycan

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11
Q

o linked glycoprotein

A

carb is linked to OH group of serine or threonine

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12
Q

n linked glycoprotein

A

carb is linked to amide group os asparagine

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13
Q

where is glycosylation common

A

in proteins that are connected to lysosomes or cell membranes

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14
Q

acetylation or methylation

A

the N terminal (first) amino acid is sometimes acelyated or methylated to change the charge on protein

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15
Q

hydroxylation

A

add OH

Hydroxylation of prolyl and Lysyl residues in collagen to hydroxyl prolyl and hydroxyl lysyl

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16
Q

hydroxylation leads to

A

stabilization of protein

17
Q

carboxylation def and example

A

adds CO2. converts glutamate to y carboxy glutamate which is important for binding of calcium

18
Q

carboxylation helps in

A

clotting factors and osteocalcin (bone protein)