Zwitterion and isoelectric point

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A zwitterion is a neutral molecule that possesses both a positive and a negative charge at different locations, while the isoelectric point (pI) is the pH at which a molecule carries no net charge. At the isoelectric point, amino acids exist as zwitterions, as the carboxyl group donates a proton to the amino group, neutralizing the overall charge. Below the isoelectric point, an excess of H+ ions leads to a positively charged molecule, while above the pI, a deficiency of H+ ions results in a negatively charged molecule. In more acidic environments below the pI, proteins can become increasingly positively charged, but the extent of this increase depends on the protein's structure and the number of protonation sites. At equilibrium, some proteins may be protonated while others are not, allowing for an average positive charge to be calculated.
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zwitterion is defined as is a neutral molecule with a positive and a negative electrical charge (n.b. not dipoles) at different locations within that molecule.

while

isoelectric point means pH at which a particular molecule or surface carries no net electrical charge.


does it mean that amino acid exist as zwitterion at isoelectric point?
 
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Yep.
 
Yeah at the isoelectric point, amino acids neutralise themselves because H+ ion from the carboxyl group bonds to the amino group. Below the IEP there is an excess of H+ ions floating around so the carboxyl group gets its proton back leaving the molecule positively charged. Above the IEP there is a deficiency of H+ ions so the acid group loses its proton leaving the molecule negatively charged.
 
So if the protein is in an environment that is below its pI, it will be positive, but the more acidic the environment becomes does the protein continue to get 'more positive'? Or does it not work like that?
 
physicsn00bie said:
So if the protein is in an environment that is below its pI, it will be positive, but the more acidic the environment becomes does the protein continue to get 'more positive'? Or does it not work like that?

To some extent it works this way. Note that protein (especially a large one) can be often protonated in more than one position. Also note that while it is impossible for a single protein to have a fractional number of protons attached, at equilibrium some proteins would be protonated and some would be not, so we can say things like "because of protonation at this pH XYZ protein has on average a positive charge of 2.35".
 
Thaaaaanks
 
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