ome ▁to ▁disc rim inate ▁on ▁proper ▁transfer ▁R NA ▁and ▁mess enger ▁R NA ▁interactions . ▁Typ ically , ▁if ▁an ▁incorrect ▁t R NA ▁pairs ▁with ▁an ▁m R NA ▁cod on ▁at ▁the ▁am ino ac yl ▁site ▁of ▁the ▁rib os ome , ▁ad en os ines ▁ 1 4 9 2 ▁and ▁ 1 4 9 3 ▁are ▁ex cluded ▁from ▁the ▁interaction ▁and ▁ret ract , ▁signal ing ▁the ▁rib os ome ▁to ▁reject ▁the ▁am ino ac yl ated ▁t R NA :: E long ation ▁F actor ▁Th ermo - Un stable ▁complex . ▁However , ▁when ▁gent am ic in ▁bind s ▁at ▁hel ix ▁ 4 4 ▁of ▁the ▁ 1 6 S ▁r R NA , ▁it ▁forces ▁the ▁ad en os ines ▁to ▁maintain ▁the ▁position ▁they ▁take ▁when ▁there ▁is ▁a ▁correct , ▁or ▁cogn ate , ▁match ▁between ▁aa - t R NA ▁and ▁m R NA . ▁This ▁leads ▁to ▁the ▁accept ance ▁of ▁incorrect ▁aa - t R N As , ▁causing ▁the ▁rib os ome ▁to ▁synth es ize ▁prote ins ▁with ▁wrong ▁am ino ▁ac ids ▁placed ▁throughout ▁( rough ly ▁every ▁ 1 ▁in ▁ 5 0 0 ). ▁The ▁non - function al , ▁m istr ans l ated ▁prote ins ▁mis fold ▁and ▁aggregate , ▁eventually ▁leading ▁to ▁death ▁of ▁the ▁b acter ium . ▁A ▁secondary ▁mechanism ▁has ▁been ▁proposed ▁based ▁on ▁cry stal ▁structures ▁of ▁gent am ic in ▁in