QUESTIONS:

1.) Possible structure that gives the positive test for the Biuret Test.

2.) Why dipeptides dont give positive result with Biuret Test.
The Biuret reagent works because the Cu2+ cupric ions form a chelating complex with peptides. It is
shaped such that four peptide bond. Nitrogen donates their electron pair to Copper. This is possible when
there are two polypeptides acting from opposite sides. With dipeptides, the orientation can never be right
because there would be just one electron pair per molecule, thus four molecules would be required, and
these bulky molecules can't huddle together around the Cu
3.) Why serine and threonine give positive results with Biuret Test

Serine and threonine as well some other chemicals are able to combine with the copper reagent to
form a ring structure which produces an intense blue color giving a positive result with Biuret
Test with no protein and interfering with the quantitative determination of the amount of protein
in protein samples with large proportions of serine and threonine. YAHOO ANS.
The Biuret Test works by forming two bidentate ligands around the copper +2 ion. Serine and
threonine both have a hydroxyl group two carbons removed from the free amino group. A lone
pair is a lone pair, so both serine and threonine can form a bidentate ligand using the amino lone
pair and the hydroxyl lone pair, giving the purple color and the false positive result.
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4.) Egg white and milk are used as antidotes for poisoning. Offer an explanation.
Heavy metal salts act to denature proteins in much the same manner as acids and bases. Heavy metal salts
usually contain Hg +2, Pb +2, Ag +1, Tl +1, Cd +2. Since salts are ionic, they disrupt salt bridges in
proteins. Thus, reaction of heavy metal salt with protein leads to an insoluble metal protein salt. As an
antidote, a protein such as milk or egg whites may be administered to precipitate the poisonous salt. Then
an emetic is given to induce vomiting so that the precipitated metal protein is discharged from the body.
5.) Picric acid and tannic acid used in treatment of burns. Offer and explanation
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6.) Nitric acid staining the skin a yellow color?

The concentrated nitric acid stains human skin yellow due to its reaction, xanthoprotein reaction, with the
protein, keratin. These yellow stains turn orange when neutralized.
7.) Difference between xanthoproteic test and heller ring test

-In the xanthoproteic test, one mixes the sample first with concentrated HNO3, then with
NH4OH. The first reaction is a color change to yellow, followed by further change to orange.
This test depends on presence of tyrosine, which has a HO-C6H4- side chain. The phenol proup
gets nitrated to nitrophenol (yellow), and the NH4OH reacts with HO- to give (-)O-C6H4-, which
is orange.
-The Heller ring test also uses nitric acid, but gives a white precipitated ring of denatured protein
where the sample, usually urine, is carefully layered over the acid.
Xanthoproteic test - used to detect the presence of proteins (will give yellow color)
Heller ring test - used for the detection of albumin in urine samples (will form precipitation or
coagulation of albumin)
Xanthoproteic test nitric acid gives a color when heated with proteins containing tyrosine
(yellow color) or tryptophan (orange color); the color is due to nitration
Heller ring test nitric acid causes denaturation of proteins with the formation of a white
precipitate

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8.) Only amino acid that contains a hydroxyphenyl group

Tyrosine

9.) Only amino acid that contains the indole group

Tryptophan

10.) In sulfur test, formula for the colored precipitate

PbS (black solid)