In aqueous media proteins carry both cationic and anionic groups on the same molecule. The ionic state
of the protein depends on the pH of the medium. A protein, rich in basic amino acids like lysine and
arginine, exists as a cation and behaves as a base at the physiological pH of 7.4 (Basic Protein) e.g.,
histones of nucleoproteins. Similarly, a protein with acidic amino acids exists as an anion and behaves
as an acid e.g., most blood proteins (Acidic Proteins).How can this be possible ???
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Explanation:
Amino acids undergo reactions characteristic of carboxylic acids and amines. The reactivity of these functional groups is particularly important in linking amino acids together to form peptides and proteins, as you will see later in this chapter. Simple chemical tests that are used to detect amino acids take advantage of the reactivity of these functional groups. An example is the ninhydrin test in which the amine functional group of α-amino acids reacts with ninhydrin to form purple-colored compounds. Ninhydrin is used to detect fingerprints because it reacts with amino acids from the proteins in skin cells transferred to the surface by the individual leaving the fingerprint.
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I don't know but I try it on Google
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