Quiz
MO17 Stability of Large Molecules
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Perguntas do quiz (5)
1Select all the degradation issues that are non-covalent.
- ADenaturation
- BAggregation
- CAdsorption
- DPrecipitation
- EDeamidation
- FOxidation
- GGlycosylation
2Choose the incorrect statement about aggregation, the formation of macromolecular complexes.
- AIt is noncovalent.
- BIt is irreversible.
- CIt happens via hydrophobic association.
- DIt is immunogenic.
- EIt does not affecting binding or activity.
- FIt could happen because of different interfaces in production, mechanical stress, interaction with metal surfaces or in the presence of other molecules
3Choose the incorrect statement about oxidation.
- AIt is covalent degradation.
- BIt occurs on multiple amino acid side chains due to oxygen, light, or peroxide
- CIt impacts stability, activity and immunogenicity
- DThe most susceptible amino acids are methionine, cysteine, tyrosine, tryptophan, and histidine
4Deamidation is a [blank_start]covalent[blank_end] degradation which happens to [blank_start]asparagine[blank_end] (Asn) and [blank_start]g;utamine[blank_end] (Gln), removing the amino group. This results in [blank_start]aspartic acid[blank_end] (Asp) and [blank_start]glutamic acid[blank_end] (Glu) respectively, and [blank_start]decreases[blank_end] the activity of the proteins.
- Acovalent
- Bnon-covalent
- Casparagine
- Dglutamine
- Easpartic acid
- Fglutamic acid
- Gdecreases
- Hincreases
5Proteolysis is a form of [blank_start]covalent[blank_end] degradation where [blank_start]proteins[blank_end] are fragmented by [blank_start]proteases[blank_end]. In acidic solutions, [blank_start]aspartic acid (Asp)[blank_end] residues are the most susceptible to hydrolysis.
- Acovalent
- Bnon-covalent
- Cproteases
- Dproteins
- Easpartic acid (Asp)
- Fglutamic acid (Glu)
Informações
- Descrição
- PHCY211 (Molecules) Quiz sobre MO17 Stability of Large Molecules, criado por Mer Scott em 13-04-2018.
- Autor
- Mer Scott
- Idioma
- English
- Visualizações
- 12
- Histórico
- Criado em 13 abr 2018 · atualizado em 13 abr 2018
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