Zwitterion and isoelectric point

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Discussion Overview

The discussion centers around the concepts of zwitterions and isoelectric points, particularly in relation to amino acids and proteins. Participants explore the conditions under which amino acids exist as zwitterions and how their charge states change with pH levels, especially in relation to their isoelectric points.

Discussion Character

  • Conceptual clarification
  • Debate/contested
  • Technical explanation

Main Points Raised

  • One participant defines zwitterions as neutral molecules with both positive and negative charges at different locations, while isoelectric point is described as the pH at which a molecule carries no net charge.
  • Another participant confirms that amino acids exist as zwitterions at their isoelectric point.
  • A participant explains that at the isoelectric point, amino acids neutralize themselves by transferring a proton from the carboxyl group to the amino group, affecting their charge based on the surrounding pH.
  • Questions arise about whether proteins become "more positive" as the environment becomes more acidic when below their isoelectric point, with a suggestion that proteins can be protonated at multiple sites.
  • It is noted that while a single protein cannot have a fractional number of protons, at equilibrium, some proteins may be protonated while others are not, leading to average charge descriptions.

Areas of Agreement / Disagreement

Participants generally agree on the relationship between zwitterions and isoelectric points, but there are uncertainties regarding the behavior of proteins in varying pH environments, indicating multiple competing views on the specifics of charge changes.

Contextual Notes

There are limitations in the discussion regarding the assumptions about protein behavior in acidic environments and the implications of protonation at multiple sites, which remain unresolved.

weng cheong
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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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