How Is the Acidity or Basicity of Amino Acids Determined?

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The acidity or basicity of amino acids is primarily determined by the pKa values of their side chains (R groups), rather than the carboxyl or amino groups, which have similar pKa values across amino acids. The pKa of the R group indicates whether an amino acid is acidic or basic, with specific amino acids exhibiting unique R group pKa values that influence their overall charge at physiological pH. If an amino acid has additional acidic groups, it would likely become more negatively charged, while more basic groups would increase its positive charge. Understanding these pKa values is crucial for predicting the behavior of amino acids in biological systems. The discussion highlights the importance of R group pKa values in determining amino acid properties.
jones106
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How can you tell if a given amino acid is acidic or basic? I'm lost here. My first thought would be to look at the pKa values. There is virtually no difference in the pKa values for the carboxyl groups; all range from 1.82-2.38. The same goes for the pKa values of the amino groups; all range from 8.8-10.96. Is it the pKa of the R group that determines whether they are acidic or basic? I'm staring at this table, and it only has pKa values for the R groups of 7 of the amino acids.

Thanks very much,
Taylor
 
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