Post Translational Modifications

Question 1

carb + OH on STY

Answer 1

o-glycosylation

Question 2

carb + NH2 of N

Answer 2

n-glycosylation

Question 3

lipid + internal SH of C

Answer 3

palmitoylation

Question 4

lipid + NH of N-terminal G

Answer 4

myristoylation

Question 5

lipid + SH of C

Answer 5

prenylation

Question 6

pi + OH of STY

Answer 6

phosphorylation

Question 7

acetyl + NH2 of K, N-terminus

Answer 7

acetylation

Question 8

ADP + N of R,Q

Answer 8

ADP-ribosylation

Question 9

P,K oxidized

Answer 9

oxidation

Question 10

carboxyl + E

Answer 10

carboxylation

Question 11

polar amino acids

Answer 11

STY CQWN

Question 12

non polar amino acids

Answer 12

FLAV GIMP

Question 13

basic amino acids

Answer 13

HKR

Question 14

acidic amino acids

Answer 14

ED

Question 15

which bonds are most susceptible to hydrolysis?

Answer 15

amides & esters between carboxylic acids

Question 16

new amino acids are always bound to which terminus?

Answer 16

C terminus (adds to the carboxyl end)

Question 17

type of bonds for 1* structure

Answer 17

covalent bonds (strong)

Question 18

type of bonds for 2* structure

Answer 18

H-bonds (permanent dipole-dipole interactions = weak)

Question 19

type of bonds for 3* structure

Answer 19

H-bonds
Disulfide bonds (covalent=strong)
LDF (partial dipoles near each other)
Ionic salt bridges (permanent dipole-dipole=strong)

Question 20

Hb protein structure

Answer 20

4* - allows it to do more because it has multiple N and C terminals

Question 21

Mb protein structure

Answer 21

3* - only has 1 N and 1 C terminal, can’t do as much as Hb

Question 22

cofactor

Answer 22

an inorganic or organic molecule required by a protein for activity (Zn++)

Question 23

coenzyme

Answer 23

an organic cofactor (NAD, FAD)

Question 24

prosthetic group

Answer 24

a tightly bound cofactor (heme)

Question 25

apoenzyme

Answer 25

protein without a cofactor

Question 26

haloenzyme

Answer 26

protein with a cofactor

Question 27

what are 2 ways to turnover proteins?

Answer 27

Lysosomal degradation

Ubiquitin post-translational modification

Question 28

where does lysosomal degradation get the proteins?

Answer 28

from outside the cell

extracellular

Question 29

whats the pH of a lysosome?

Answer 29

ph 6 - mimics the stomach

Question 30

what is cathepsin?

Answer 30

family of proteases that denatures proteins that are shuttle to the lysosome

breaks proteins into amino acids that the cell can use again

Question 31

autophagy

Answer 31

whole organelle turnover

Question 32

what LSD disease is related to protein degradation?

Answer 32

pycnodysososis (cathepsin K mutation)

Question 33

what LSD disease is related to glycogen degradation?

Answer 33

pompe disease

Question 34

what LSD diseases are related to sphingolipid degradation?

Answer 34

• Gaucher
• Tay Sachs
• Niemann Pick

Question 35

what does the ubiquitin protein covalently link to?

Answer 35

amine side chain of K residues

Question 36

how many amino acids are in ubiquitin?

Answer 36

76