A simple diagram showing the strategy for drug-dependent epitope tagging of newly synthesized proteins can be found here: [1].

These processes load newly synthesized histones onto DNA.

However, newly synthesized proteins may not fold correctly, or properly folded proteins can spontaneously misfold.

Newly synthesized structural proteins and genomes would self-assemble and accumulate near the inside of the cell membrane.

The challenge that arises is how to get specific, newly synthesized proteins to the correct input-specific synapses they are need at.

These newly synthesized membranes do not come from the thylakoids, but rather from vesicles generated from the inner membrane of the plastid.

These newly synthesized viral particles are subsequently transported through the plasmodesmata to adjacent plant cells via several assisting potyvirus proteins.

Although most newly synthesized proteins can fold in absence of chaperones, a minority strictly requires them for the same.

The strand displacement generates newly synthesized single stranded DNA template for more primers to anneal.

The field is very active, with newly synthesized and tested compounds reported weekly in prominent research journals.