Test
Physical Modifications
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Preguntas del test (33)
1Physical modifications are reversible
- AVerdadero
- BFalso
2Give an example of protein oxidation
- ADisulphide bond formation
- BHydrogen bond formation
- CGlycosylation
3Where are proteins with oxidated modifications are nearly universally found where?
- AOutside the cell
- BThe cytoplasm
- CNucleus
- DI.e. Oxidative environments
4What is so useful about disulphide bonds?
- AThey're heat stable
- BThey're protease resitant
- CThey're structurally resilient
5Where do oxidation reactions occur?
- AThe golgi
- BThe ER
- CThe ribosome
6Disulphide bonds assist in recovery from denaturation
- AVerdadero
- BFalso
7In Maristoylation, what is added?
- AMaristic acid
- BMaristoylate
- CMaristoyl-3-phosphate
8Describe the substrate added in Myristoylation
- A4C
- B5C
- C6C
- DSaturated & hydrophobic
- EUnsaturated & hydrophilic
9What is the point of Myristoylation?
- AIt polarises a protein
- BIt binds a protein to a membrane
- CIt binds two ends of a protein together
10What sequence is the Myristoylation substrated added to?
- AThe N-terminus
- BThe C-terminus
- CMGXXX(T/S)
- DMPXXX(G/F)
- ESDXXX(S/R)
11The protein that performs Myristoylation is N-Myristoyl transferase
- AVerdadero
- BFalso
12How is the Myristoylation substrate added?
- AFirst the phenylalinine is removed
- BFirst the methionine is removed
- CFirst the tyrosine is removed
- DThen the substrate is added to the glycine
- EThen the substrate is added to the leucine
- FThen the substrate is added to the isoleucine
13Prenylation is the addition of ketones
- AVerdadero
- BFalso
14Name the two substrates most often added in prenylation
- AFarnesyl
- BGeranylgeranyl
- CDerisyl
- DNitrosyl
15Where does prenylation occur?
- AIn a CAAX box (where A should be Alanine, but anything small and hydrophobic will do)
- BIn a FAAX box (where A should be Isoleucine, but anything small and hydrophobic will do)
- CIn a CAAT box (where A should be Alanine, but anything small and hydrophobic will do)
16In prenylation, the X of the sequence must be the terminal aa of the chain
- AVerdadero
- BFalso
17Put 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- AA-C-B
- BB-C-A
- CA-B-C
18Prenylation is done to proteins destined for the cytoplasm
- AVerdadero
- BFalso
19Name the types of glycosylation
- AN-linked
- BO-linked
- CC-Mannosylation
- DPhosphoserine Linked
20Glycosylation is the addition of carbohydrate chains
- AVerdadero
- BFalso
21What is the site of N-linked glycosylation?
- AThe Asn in an NX(S/T)
- BThe Phe in an FX(S/T)
- CThe Gly in a GX(S/T)
22What is the residue that is attached to the amino acid?
- AMannose
- BGlucose
- CN-acetyl-galactosamine
- DN-acetyl glucosamine
23What residues are on the tips of the branches?
- AMannose
- BGlucose
- CFructose
24If the branches end with mannose, what is the process called?
- AHigh-mannose Biantennary N-glycosylation
- BHigh-mannose N-glycosylation
- CMannosylation
25Why are 3 glucose added to the sugar complex in the golgi?
- ASo they can be removed as markers for protein folding and transport
- BSo the Golgi knows they're bound for the membrane
- CSo the Golgi can degrade the protein as faulty
26Why is it called High-Mannose Biantennary N-Glycosylation?
- ABecause one of the three branches is removed, giving two 'antenna'
- BBecause another branch is formed off the first one, giving two 'antenna'
- CBecause proteins with this type of glycosylation act as receptor proteins with two antenna
27Once the Biantennary complex has been formed, what happens next?
- AMannose is removed
- BAddition of N-acetyl neuraminic acids
- CAddition of glucose
- DRemoval of N-acetyl glucosamine
- EAddition of a fucose to the GlcNac bound to the amino acid
28Why the complicated process of adding and removing sugars?
- AIt adds a date stamp to the cell- over time the NeuAc's fall off, which signals the protein for degredation
- BIt adds a transport signal- depending on what is added or removed, proteins are directed to different areas by carrier proteins
- CIt's quality control- the contortions required to add and remove all the sugars mean that the protein has folded properly
29The HIV virus can use glycosylation to hide from the immune system
- AVerdadero
- BFalso
30Why is N-linked glycosylation potentially dangerous?
- ABecause the immune system is programmed to ignore it, viral coat proteins can use it to hide the virus
- BBecause NeuAc's can be toxic in high concentrations
- CBecause the removal of mannose can cause the protein to misfold
31HIV1-gp120 has many N-X-(T/S) sequences to be glycosylated
- AVerdadero
- BFalso
32Where does HIV1-gp120 bind?
- ACD4 receptor
- BCD8 receptor
- CB-lymphocyte receptors
33How does the HIV virus invade the lyphocyte?
- AIt's only glycosylated on a very small binding site
- BIt's only not glycosylated on a very small binding site
- CWhich allows it to bind and invade
Información
- Descripción
- (Protein Modifications) Structural Basis for Biological Function Test sobre Physical Modifications, creado por gina_evans0312 el 21/12/2013.
- Autor
- gina_evans0312
- Idioma
- English
- Visitas
- 474
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