I have serine aa in the core of protein behaving as a positive entity which i inferred from electropotential surface. as it contain OH negative its should behave as negative entity. I am not able to understand the reason behind this behavior.
The hydrogen atom in serine's OH group has a partial acidic character, i.e. it is behaving as a proton. Indeed, in serine proteases OH loses a proton and the oxygen acts as a nucleophile.