When ammonia or primary and secondary amines are detected, a deep blue or purple color known as Ruhemann's purple is produced.
Ninhydrin can also be used to monitor deprotection in solid phase peptide synthesis (Kaiser Test). The chain is linked via its C-terminus to the solid support, with the N-terminus extending off it. When that nitrogen is deprotected, a ninhydrin test yields blue. Amino-acid residues are attached with their N-terminus protected, so if the next residue has been successfully coupled onto the chain, the test gives a colorless or yellow result.
Most of the amino acids are hydrolyzed and reacted with ninhydrin except proline. So proline forms yellow color with ninhydrin.
These are the amino acids that will yield positive result to the ninhydrin test: Non-polar amino acids: Glycine, Alanine, Valine, Leucine, Isoleucine, Phenylalanine, Methionine, Tryptophan Polar Neutral Amino acids: Serine, Cysteine, Threonine, Asparagine, Glutamine, Tyrosine Polar Acidic Amino Acids: Aspartic acid and Glutamic acid Polar Basic Amino Acids: Histidine, Lysine, Arginine
proline!
Since amino acids are colourless compounds, ninhydrin is used for detecting them. To identify this, after development, the TLC plate is sprayed with ninhydrin reagent and dried in an oven, at 105°C for about 5 minutes. Ninhydrin reacts with α- amino acids that results in purple coloured spots [(due to the formation of the complex - Rheuman's purple).
Kharkov's
338.4 °C, 612 K or 641 °F
Ninhydrin reacts with proline to give a red colored product
Yes. Within "The Chemical Reactions of Amino Acids / Reactions of Amino Groups" there are several examples - one of which is the ninhydrin reaction. A very widely applied reaction of the alpha amino group [that is the N in the peptide bond -CCN-CCN-], it is used to estimate the quantity of amino acids [in a sample] in very small amounts. All amino acids and polypeptides with a free alpha group react with ninhydrin and yield [or produce] an intensely purple colored product - except for Proline and Hydroxyproline {both in which the alpha amino group is termed to be 'substituted' - something to do with carbon rings} which "yield derivatives with a characteristic yellow color." See also 'Schiff's bases'.
It would be the amine group. In fact, ninhydrin will react with other amines, not necessarily those in proteins or amino acids. it reacts with free amines to produce blue-purple color and yellow in proline.
These are the amino acids that will yield positive result to the ninhydrin test: Non-polar amino acids: Glycine, Alanine, Valine, Leucine, Isoleucine, Phenylalanine, Methionine, Tryptophan Polar Neutral Amino acids: Serine, Cysteine, Threonine, Asparagine, Glutamine, Tyrosine Polar Acidic Amino Acids: Aspartic acid and Glutamic acid Polar Basic Amino Acids: Histidine, Lysine, Arginine
Ninhydrin is used in amino acid TLC because it readily stains amino acids by reacting with the amine groups. This reaction takes place very quickly and creates a brownish-color that can be easily visualized.
NO, ninhydrin is not the same as super glue
Yes ninhydrin does have flaws. The most common flaw of ninhydrin is the fact that it is so sensitive to the extent of not recording a fingerprint if enough perspiration wasn't created.
proline!
Well, the best I could come up with is it's either:C9H6O2orC4H3O2If someone knows any different please correct me.jman63: it is actually C9H6O4
Since it's a secondary α-amino acid that doesn't have a free amino group
Since amino acids are colourless compounds, ninhydrin is used for detecting them. To identify this, after development, the TLC plate is sprayed with ninhydrin reagent and dried in an oven, at 105°C for about 5 minutes. Ninhydrin reacts with α- amino acids that results in purple coloured spots [(due to the formation of the complex - Rheuman's purple).
You can find proline(an amino acid that produces collagen and cartilage) in glutamic acid.