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Membrane bound organelles

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Total cards: 22•Content version: v4•Public deck•Updated: 8/1/2026

Card preview (22)

#1
Front (Question)

what did the nuclear genome of a eukaryotic cell evolve from

Back (Answer)

ancient archeaon

#2
Front (Question)

evolution of mitochondria

Back (Answer)

anaerobic archea formed symbiotic relationship with bacteria and the bacteria evolved into mitochondria

#3
Front (Question)

function of peroxisomes

Back (Answer)

fatty acid beta oxidation

#4
Front (Question)

what is the endomembrane system

Back (Answer)

Topologically equivalent compartments in the secretory and endocytic pathways in a eukaryotic cell molecules can get from one to the other without crossing a membrane via vesicles

#5
Front (Question)

which organelles are in the endomembrane system

Back (Answer)

ER plasma membrane lysosome nuclear envelope golgi body endosomes vesicles they are separate from the cytoplasm equivalent to external environment

#6
Front (Question)

role of translocons in ER membrane

Back (Answer)

protein conducting channels as a protein is being synthesised, it gets pushed into the lumen of the ER via these channels

#7
Front (Question)

which side of the ER membrane does protein synthesis occur

Back (Answer)

cytoplasmic

#8
Front (Question)

what is N-glycosylation

Back (Answer)

attachment of an oligosaccharide to specific asparagine amino acids in the polypeptide that are part of: Asn-X-Ser, or Asn-X-Thr where X can be any amino acid except proline

#9
Front (Question)

where is the oligosaccharide anchored

Back (Answer)

covalently linked to dolichol lipid anchor in ER membrane

#10
Front (Question)

how is the oligosaccharide transferred to the protein

Back (Answer)

catalysed by oligosaccaryl transferase transfers it as a single unit

#11
Front (Question)

which proteins does N-glycosylation occur to

Back (Answer)

ones that go into ER lumen (not cytosilic proteins)

#12
Front (Question)

glucose trimming

Back (Answer)

glucose residues in oligosaccharide added trimmed by glucosidases, preparing the protein for folding

#13
Front (Question)

what happens to incompletely folded proteins

Back (Answer)

undergoes cycle of glucose addition and removal glucosyl transferase adds glucose back to the oligosaccharide to mark it for another round of folding attempts

#14
Front (Question)

calnexin binding

Back (Answer)

chaperone protein helps protein fold correctly by stabilising the intermediate states of the folding process

#15
Front (Question)

glucosidase action

Back (Answer)

removes glucose after aid by calnexin signal for protein to be checked again for proper folding misfolded or missambled proteins do not leave the ER

#16
Front (Question)

why do few disulfide bridges form in the cytoplasm but many form in the ER lumen

Back (Answer)

cytoplasm is a reducing environment lumen of ER is an oxidising environment protein disulfide isomerases

#17
Front (Question)

organisation of the golgi apparatus

Back (Answer)

divided into multiple cisternae that contain different enzymes that carry out sequential modifications of proteins as they move through

#18
Front (Question)

constitutive secretion

Back (Answer)

no signal needed continuous process

#19
Front (Question)

regulated secretion

Back (Answer)

storage of secretory vesicles within the cell until an external signal triggers their release

#20
Front (Question)

O linked glycosylation

Back (Answer)

addition of sugars onto the oxygen of hydroxyl groups of serine and threonine residues in proteins. occurs in golgi apparatus

#21
Front (Question)

A blood group antigen

Back (Answer)

enzyme adds N-acetylgalactosamine

#22
Front (Question)

B blood group antigen

Back (Answer)

enzyme adds galactose