Explain how hydrogen bonding occurs between amino acids?
Nitrogen and Oxygen are both very electronegative elements, making the C=O and N-H bonds are polar. This leads to the formation of a hydrogen bond between O and H, in which the lonepair of electrons on an O atom is strongly attracted to the δ+H atom in another amino acid
the acid-base behaviour of amino acids?
amino acids exist as zwitterions, with the amine part represented as NH3+, and the carboxyl group as COO-
in acid conditions, the COO- is protonated, turning into COOH, this makes an overall positive ion
in basic conditions, a hydrogen is removed from the NH3+, making an overall negative ion