Amino acids 

are molecules containing an amine group, a carboxylic acid group and a

side chain that varies between different amino acids. These molecules contain the key elements
of carbon, hydrogen, oxygen, and nitrogen. These molecules are particularly important
in biochemistry, where this term usually refers to alpha-amino acids with the general formula
H2NCHRCOOH. Amino acids are the building blocks of proteins. 20 different amino acids are used to
synthesize proteins. The shape and other properties of each protein are dictated by the precise
sequence of amino acids in it.

An essential or indispensable amino acid cannot be made by the body and must be
supplied by food. These include isoleucine, leucine, lysine, methionine
phenylalanine, threonine, tryptophan, and valine. Another amino acid - histidine is considered semi-
essential because the body does not always require dietary sources of it. Nonessential amino acids are
made by the body from the essential amino acids or normal breakdown of proteins. The nonessential
amino acids are arginine, alanine, asparagine, aspartic acid, cysteine, glutamine, glutamic
acid, glycine, proline, serine, and tyrosine. The twenty amino each have assigned to them both three-
letter and one-letter codes.

The biuret test is a chemical test used for detecting the presence of peptide bonds. In
the presence of peptides, a copper(II) ion forms a violet-colored complex in an alkaline solution.[1]
Several variants on the test have been developed.The Biuret reaction can be used to assay the
concentration of proteins because peptide bonds occur with the same frequency per amino acid in the
peptide. The intensity of the color, and hence the absorption at 540 nm, is directly proportional to the
protein concentration, according to the Beer-Lambert law.In spite of its name, the reagent does not in
fact contain biuret ((H2N-CO-)2NH). The test is so named because it also gives a positive reaction to
the peptide bonds in the biuret molecule.

Xanthoproteic acid test is a chemical test for specific functional groups in amino
acid side chains that gives a color with only two of the twenty amino acids, tyrosine and tryptophan.
Depending which is present, formation of a yellow or orange color is a positive test. They are to add 5
drops of concentrated nitric acid to 10 drops of two amino acid solutions, either 0.02% tryptophan or
0.005% tyrosine (may need a bit of NaOH to dissolve); tubes should be quite dry since even a few
drops of water may dilute the nitric acid enough to prevent nitration. After heating in a boiling water
bath for five minutes, students add 25-30 drops of 3 M NaOH and note the final color formed.
Tyrosine should be yellow and tryptophan orange.

Ninhydrin (2,2-Dihydroxyindane-1,3-dione) is a chemical used to detect ammonia

or primary and secondary amines. When reacting with these free amines, a deep blue or purple color
known as Ruhemann's purple is produced. Ninhydrin is most commonly used to detect fingerprints, as
the terminal amines or lysine residues in peptides and proteins sloughed off in fingerprints react with
ninhydrin. The Sakaguchi test is a specific qualitative test for the detection of a specific type of protein
with the amino acid containing the guanidinium group. In basic conditions, alpha naphthol and sodium
hypobromite/chlorite react with the aforementioned compound to form red-orange complexes.

The hopkins-cole test determines the presence of amino acid tryptophan. Some
chemists no longer will use the hopkins-cole test becasuse it is not completely understood' in terms of
chemistry. The tryptophan that the hopkins-cole test determines can be defined as an indole nucleus.
The tryptophan creates the violet ring where the two layers meet.

The lead acetate has heavy metal Pb that irreversibly denatures the proteins, and
even after dilution with water the white precipitate remains

The Sakaguchi test is used to test for a certain amino acid and proteins. The amino
acid that is detected in this test is arginine. The sample to be tested is treated with alpha-naphthol and
sodium hypochlorite. A positive result yields a reddish wine color when arginine is present. The
reagents used in this test are dangerous
Physicochemical properties of amino acids

The 20 amino acids encoded directly by the genetic code can be divided into several groups based on their
properties. Important factors are charge, hydrophilicity or hydrophobicity, size and functional groups.[9] These
properties are important for protein structure and protein–protein interactions. The water-soluble proteins tend to
have their hydrophobic residues (Leu, Ile, Val, Phe and Trp) buried in the middle of the protein, whereas hydrophilic
side chains are exposed to the aqueous solvent. The integral membrane proteins tend to have outer rings of exposed
hydrophobic amino acids that anchor them into the lipid bilayer. In the case part-way between these two extremes,
some peripheral membrane proteins have a patch of hydrophobic amino acids on their surface that locks onto the
membrane. Similarly, proteins that have to bind to positively-charged molecules have surfaces rich with negatively
charged amino acids like glutamate and aspartate, while proteins binding to negatively-charged molecules have
surfaces rich with positively charged chains like lysine and arginine. There are different hydrophobicity scales of
amino acid residues.[85]

Some amino acids have special properties such as cysteine, that can form covalent disulfide bonds to other cysteine
residues, proline that forms a cycle to the polypeptide backbone, and glycine that is more flexible than other amino
acids.

Zwitterions

Amino acids have both amine and carboxylic acid functional groups and are therefore both an acid and a base at the
same time.[9] At a certain pH known as the isoelectric point an amino acid has no overall charge, since the number of
protonated ammonia groups (positive charges) and deprotonated carboxylate groups (negative charges) are equal.[18]
The amino acids all have different isoelectric points. The ions produced at the isoelectric point have both positive
and negative charges and are known as a zwitterion, which comes from the German word Zwitter meaning
"hermaphrodite" or "hybrid".[19] Amino acids can exist as zwitterions in solids and in polar solutions such as water,
but not in the gas phase.[20] Zwitterions have minimal solubility at their isolectric point and an amino acid can be
isolated by precipitating it from water by adjusting the pH to its particular isoelectric point.