Physical Modifications

Descrição

Structural Basis for Biological Function (Protein Modifications) Quiz sobre Physical Modifications, criado por gina_evans0312 em 21-12-2013.
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Quiz por gina_evans0312, atualizado more than 1 year ago
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Criado por gina_evans0312 quase 11 anos atrás
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Resumo de Recurso

Questão 1

Questão
Physical modifications are reversible
Responda
  • True
  • False

Questão 2

Questão
Give an example of protein oxidation
Responda
  • Disulphide bond formation
  • Hydrogen bond formation
  • Glycosylation

Questão 3

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

Questão 4

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

Questão 5

Questão
Where do oxidation reactions occur?
Responda
  • The golgi
  • The ER
  • The ribosome

Questão 6

Questão
Disulphide bonds assist in recovery from denaturation
Responda
  • True
  • False

Questão 7

Questão
In Maristoylation, what is added?
Responda
  • Maristic acid
  • Maristoylate
  • Maristoyl-3-phosphate

Questão 8

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

Questão 9

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

Questão 10

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

Questão 11

Questão
The protein that performs Myristoylation is N-Myristoyl transferase
Responda
  • True
  • False

Questão 12

Questão
How is the Myristoylation substrate added?
Responda
  • 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

Questão 13

Questão
Prenylation is the addition of ketones
Responda
  • True
  • False

Questão 14

Questão
Name the two substrates most often added in prenylation
Responda
  • Farnesyl
  • Geranylgeranyl
  • Derisyl
  • Nitrosyl

Questão 15

Questão
Where does prenylation occur?
Responda
  • 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)

Questão 16

Questão
In prenylation, the X of the sequence must be the terminal aa of the chain
Responda
  • True
  • False

Questão 17

Questão
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
Responda
  • A-C-B
  • B-C-A
  • A-B-C

Questão 18

Questão
Prenylation is done to proteins destined for the cytoplasm
Responda
  • True
  • False

Questão 19

Questão
Name the types of glycosylation
Responda
  • N-linked
  • O-linked
  • C-Mannosylation
  • Phosphoserine Linked

Questão 20

Questão
Glycosylation is the addition of carbohydrate chains
Responda
  • True
  • False

Questão 21

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

Questão 22

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

Questão 23

Questão
What residues are on the tips of the branches?
Responda
  • Mannose
  • Glucose
  • Fructose

Questão 24

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

Questão 25

Questão
Why are 3 glucose added to the sugar complex in the golgi?
Responda
  • 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

Questão 26

Questão
Why is it called High-Mannose Biantennary N-Glycosylation?
Responda
  • 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

Questão 27

Questão
Once the Biantennary complex has been formed, what happens next?
Responda
  • 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

Questão 28

Questão
Why the complicated process of adding and removing sugars?
Responda
  • 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

Questão 29

Questão
The HIV virus can use glycosylation to hide from the immune system
Responda
  • True
  • False

Questão 30

Questão
Why is N-linked glycosylation potentially dangerous?
Responda
  • 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

Questão 31

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

Questão 32

Questão
Where does HIV1-gp120 bind?
Responda
  • CD4 receptor
  • CD8 receptor
  • B-lymphocyte receptors

Questão 33

Questão
How does the HIV virus invade the lyphocyte?
Responda
  • 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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