Practice Questions

LHCs are pigment-protein chromoprotein complexes where chlorophylls and carotenoids are precisely bound to a protein matrix to capture light.

Without N-linked oligosaccharide chains, nascent polypeptides inside the ER lumen cannot fold properly, triggering the unfolded protein response.

The central axis of a proteoglycan monomer is a core protein, from which numerous long glycosaminoglycan chains extend outwards.

Ferritin is a hollow metalloprotein shell that stores iron atoms safely as ferric oxide mineral cores, preventing oxidative cellular damage.

Many nucleoporins are modified with single O-linked N-acetylglucosamine (O-GlcNAc) residues, which are essential for pore function and transport regulation.

Lipidation, such as prenylation or palmitoylation, adds a hydrophobic lipid tail to a protein, anchoring it into a lipid bilayer.

Genetic variations dictate which glycosyltransferase is active, determining whether an extra N-acetylgalactosamine (A) or galactose (B) is added.

Spliceosomes are specialized ribonucleoproteins; they require small nuclear RNAs to recognize splice sites on pre-mRNA transcripts.

Lipoprotein lipase hydrolyzes the triacylglycerols inside circulating chylomicrons and VLDLs, releasing free fatty acids for tissue uptake.

Cancer cells alter their surface glycosylation profiles, which helps them evade immune detection and metastasize to other tissues.