The phenomenon you described does exist[0], and similar effects (though rarely as severe) in cotranslational folding have been known for some time now. AFAIK it's not studied that intensely, as it's hard to study experimentally, and it is not expected to have a significant effect on final protein folding. During the folding process proteins often undergo partial misfolds, and defold again (the protein is basically doing a gradient descent search for the lowest energy state), so a small misfold at the beginning of the the translation process will rarely make it into the final fold.

Apart from protein folding there are other interfering folding mechanisms like chaperone proteins that also make it hard to phrase it as a straight "sequence -> structure" prediction problem, though they often only exist for a small number of the total proteins (in humans).

[0]: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5737824/