Physical Modifications

Description

Structural Basis for Biological Function (Protein Modifications) Quiz on Physical Modifications, created by gina_evans0312 on 21/12/2013.
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Quiz by gina_evans0312, updated more than 1 year ago
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Created by gina_evans0312 over 10 years ago
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Resource summary

Question 1

Question
Physical modifications are reversible
Answer
  • True
  • False

Question 2

Question
Give an example of protein oxidation
Answer
  • Disulphide bond formation
  • Hydrogen bond formation
  • Glycosylation

Question 3

Question
Where are proteins with oxidated modifications are nearly universally found where?
Answer
  • Outside the cell
  • The cytoplasm
  • Nucleus
  • I.e. Oxidative environments

Question 4

Question
What is so useful about disulphide bonds?
Answer
  • They're heat stable
  • They're protease resitant
  • They're structurally resilient

Question 5

Question
Where do oxidation reactions occur?
Answer
  • The golgi
  • The ER
  • The ribosome

Question 6

Question
Disulphide bonds assist in recovery from denaturation
Answer
  • True
  • False

Question 7

Question
In Maristoylation, what is added?
Answer
  • Maristic acid
  • Maristoylate
  • Maristoyl-3-phosphate

Question 8

Question
Describe the substrate added in Myristoylation
Answer
  • 4C
  • 5C
  • 6C
  • Saturated & hydrophobic
  • Unsaturated & hydrophilic

Question 9

Question
What is the point of Myristoylation?
Answer
  • It polarises a protein
  • It binds a protein to a membrane
  • It binds two ends of a protein together

Question 10

Question
What sequence is the Myristoylation substrated added to?
Answer
  • The N-terminus
  • The C-terminus
  • MGXXX(T/S)
  • MPXXX(G/F)
  • SDXXX(S/R)

Question 11

Question
The protein that performs Myristoylation is N-Myristoyl transferase
Answer
  • True
  • False

Question 12

Question
How is the Myristoylation substrate added?
Answer
  • First the phenylalinine is removed
  • First the methionine is removed
  • First the tyrosine is removed
  • Then the substrate is added to the glycine
  • Then the substrate is added to the leucine
  • Then the substrate is added to the isoleucine

Question 13

Question
Prenylation is the addition of ketones
Answer
  • True
  • False

Question 14

Question
Name the two substrates most often added in prenylation
Answer
  • Farnesyl
  • Geranylgeranyl
  • Derisyl
  • Nitrosyl

Question 15

Question
Where does prenylation occur?
Answer
  • In a CAAX box (where A should be Alanine, but anything small and hydrophobic will do)
  • In a FAAX box (where A should be Isoleucine, but anything small and hydrophobic will do)
  • In a CAAT box (where A should be Alanine, but anything small and hydrophobic will do)

Question 16

Question
In prenylation, the X of the sequence must be the terminal aa of the chain
Answer
  • True
  • False

Question 17

Question
Put the following in order A- The COOH group is modified to a methyl group to make it uncharged B- The substrate is added to the cystine C- The last three aa are removed
Answer
  • A-C-B
  • B-C-A
  • A-B-C

Question 18

Question
Prenylation is done to proteins destined for the cytoplasm
Answer
  • True
  • False

Question 19

Question
Name the types of glycosylation
Answer
  • N-linked
  • O-linked
  • C-Mannosylation
  • Phosphoserine Linked

Question 20

Question
Glycosylation is the addition of carbohydrate chains
Answer
  • True
  • False

Question 21

Question
What is the site of N-linked glycosylation?
Answer
  • The Asn in an NX(S/T)
  • The Phe in an FX(S/T)
  • The Gly in a GX(S/T)

Question 22

Question
What is the residue that is attached to the amino acid?
Answer
  • Mannose
  • Glucose
  • N-acetyl-galactosamine
  • N-acetyl glucosamine

Question 23

Question
What residues are on the tips of the branches?
Answer
  • Mannose
  • Glucose
  • Fructose

Question 24

Question
If the branches end with mannose, what is the process called?
Answer
  • High-mannose Biantennary N-glycosylation
  • High-mannose N-glycosylation
  • Mannosylation

Question 25

Question
Why are 3 glucose added to the sugar complex in the golgi?
Answer
  • So they can be removed as markers for protein folding and transport
  • So the Golgi knows they're bound for the membrane
  • So the Golgi can degrade the protein as faulty

Question 26

Question
Why is it called High-Mannose Biantennary N-Glycosylation?
Answer
  • Because one of the three branches is removed, giving two 'antenna'
  • Because another branch is formed off the first one, giving two 'antenna'
  • Because proteins with this type of glycosylation act as receptor proteins with two antenna

Question 27

Question
Once the Biantennary complex has been formed, what happens next?
Answer
  • Mannose is removed
  • Addition of N-acetyl neuraminic acids
  • Addition of glucose
  • Removal of N-acetyl glucosamine
  • Addition of a fucose to the GlcNac bound to the amino acid

Question 28

Question
Why the complicated process of adding and removing sugars?
Answer
  • It adds a date stamp to the cell- over time the NeuAc's fall off, which signals the protein for degredation
  • It adds a transport signal- depending on what is added or removed, proteins are directed to different areas by carrier proteins
  • It's quality control- the contortions required to add and remove all the sugars mean that the protein has folded properly

Question 29

Question
The HIV virus can use glycosylation to hide from the immune system
Answer
  • True
  • False

Question 30

Question
Why is N-linked glycosylation potentially dangerous?
Answer
  • Because the immune system is programmed to ignore it, viral coat proteins can use it to hide the virus
  • Because NeuAc's can be toxic in high concentrations
  • Because the removal of mannose can cause the protein to misfold

Question 31

Question
HIV1-gp120 has many N-X-(T/S) sequences to be glycosylated
Answer
  • True
  • False

Question 32

Question
Where does HIV1-gp120 bind?
Answer
  • CD4 receptor
  • CD8 receptor
  • B-lymphocyte receptors

Question 33

Question
How does the HIV virus invade the lyphocyte?
Answer
  • It's only glycosylated on a very small binding site
  • It's only not glycosylated on a very small binding site
  • Which allows it to bind and invade
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