Can someone explain to me why the carboxylic acid group and the amino group both have charges on them in neutral water? The pKa for carboxylic acid is around 2-5 depending on its enviroment. I am confused that a pKa of 2.3 would give a ratio of 80000 deprotonated to 1 protonated? If the acid has a pKa it means it is weak, a pKa of 2.3 gives a concentration lower than 1. I assume the majority would be protonated. But all info I read states that the majority is deprotonated at a pH of 7. Can someone explain why to me it is this way? Thank you!