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Amino Acid Titration  
 
   
Amino Acid Titration
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  Titration Behavior of Amino Acids
Titration Behavior of Amino Acids
  Amino acids are polyprotic, i.e., they all contain two or three dissociable protons. As a biochemistry student, you will be capable of more precise and quantative analysis of polypeptides and proteins, and their associated functions, if you can accurately analyze the titration behavior of the amino acid side chains.  
  Natural Amino Acids
Natural Amino Acids
  The twenty alpha-amino acids are the primary components of proteins, their incorporation being governed by the genetic code. Many other naturally occurring amino acids exist, and the structures of a few of these are displayed below. Some, such as hydroxylysine and hydroxyproline, are simply functionalized derivatives of a previously described compound.  
  Amine Acylation
Natural α-Amino Acids
  Hydrolysis of proteins by boiling aqueous acid or base yields an assortment of small molecules identified as α-aminocarboxylic acids. More than twenty such components have been isolated, and the most common of these are listed in the following table. Those amino acids having green colored names are essential diet components, since they are not synthesized by human metabolic processes.  
  Natural Amino Acids
Amine Acylation
  In order to convert the amine function of an amino acid into an amide, the pH of the solution must be raised to 10 or higher so that free amine nucleophiles are present in the reaction system. Carboxylic acids are all converted to carboxylate anions at such a high pH, and do not interfere with amine acylation reactions.  
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