DEPARTMENT OF PURE AND APPLIED CHEMISTRY

COLLEGE OF ARTS AND SCIENCES

Visayas State University

Visca, Baybay City, Leyte

Name: Bebanco, Mary Grace Z. Date Performed: June 19, 2019

Group No. : 1 Date Submitted: July 1, 2019
Instructor: Marina Angela M. Teleron Score:

Experiment No. 5

AMINO ACIDS

I. INTRODUCTION

An amino acid is a type of organic acid that contains a carboxyl functional group (-COOH)
and an amine functional group (-NH2) as well as a side chain (designated as R) that is specific to the
individual amino acid. Amino acids are considered to be the building blocks of polypeptides and
proteins. The elements found in all amino acids are carbon, hydrogen, oxygen, and nitrogen. Amino
acids may contain other elements on their side chains.
The name “amino acid” is derived from the amino group and carboxyl-acid-group in their basic
structure. There are 21 amino acids present in proteins, each with a specific R group or side chain. The
21st amino acid is selenocysteine, with an R group of -CH2-SeH. Ten of these are considered essential
amino acids in humans because the human body cannot produce them and they must be obtained from
the diet. All organisms have different essential amino acids based on their physiology.
Shorthand notation for amino acids may be either a three-letter abbreviation or a single letter. For
example, Asparagine may be indicated by N or Asn; Phenylalanine is F or Phe; Glycine is G or Gly.
Amino acids may function on their own, but more commonly act as monomers to form
larger molecules. Linking a few amino acids forms peptides. A chain of many amino acids is called a
polypeptide. Polypeptides may become proteins.
The process of producing proteins based on an RNA template is called translation.
Translation occurs in ribosomes of cells. There are 22 amino acids involved in protein production.
These amino acids are considered to be proteinogenic. In addition to the proteinogenic amino acids,
there are some amino acids that are not found in any protein. An example is the neurotransmitter
gamma-aminobutyric acid. Typically, nonproteinogenic amino acids function in amino acid metabolism.
The translation of the genetic code involves 20 amino acids, which are called canonical
amino acids or standard amino acids. For each amino acid, a series of three mRNA residues acts as a
codon during translation (the genetic code). The other two amino acids found in proteins are
pyrrolysine and selenocysteine. These two amino acids are specially coded, usually by an mRNA codon
that otherwise functions as a stop codon.
II. RESULTS AND DISCUSSIONS

A. Structure of Amino Acids

(Gly) (Gly)

(Glycylglycine)

When two amino acids are joined together, a dipeptide is formed. A special chemical bond called
a peptide bond holds together two amino acids. Based on the figure above, when two glycine molecules
was joined together by a peptide bond, a glycylglycine is formed which is a dipeptide. A water molecule
was released during the process.

B. pH of Amino Acids

Amino Acid pH Structure Explanation

Alanine (A/Ala). Important source of energy
for muscle. One of the three most important
Alanine 7.2 glycogenic amino acids. The primary amino acid in
sugar metabolism. Boosts immune system by
producing antibodies.

Cysteine (C/Cys). Protective against

Cysteine 7.2 radiation, pollution and ultra-violet light. Detoxifier,
necessary for growth and repair of skin.

Glutamate (E/Glu). Neurotransmitter that is

Glutamic Acid 3.4 involved in DNA synthesis.

Tyrosine (Y/Tyr). Precursor of dopamine,

norepinephrine and adrenaline. Increases energy,
Tyrosine 6.5 improves mental clarity and concentration, can treat
some depressions.
 Aspartate (D/Asp). Increases stamina and
Aspartic Acid 3.1 helps protect the liver; DNA and RNA metabolism,
immune system function.

Valine (V/Val). Essential for muscle

Valine 5.5 development.

Amino acids have different pH levels. The non-polar amino acids like alanine and valine had a pH
value of 7.2 and 5.5, respectively. Tyrosine having a pH of 6.5 and cysteine with pH value of 7.2, were both
uncharged polar group. Glutamic acid and Aspartic acid which were acidic amino acids had a pH of 3.4 and
3.1, respectively.

C. Paper Chromatography
Calculations: Rf Values

𝑑𝑖𝑠𝑡𝑎𝑛𝑐𝑒 𝑡𝑟𝑎𝑣𝑒𝑙𝑒𝑑 𝑏𝑦 𝑎𝑚𝑖𝑛𝑜 𝑎𝑐𝑖𝑑

Rf = 𝑑𝑖𝑠𝑡𝑎𝑛𝑐𝑒 𝑡𝑟𝑎𝑣𝑒𝑙𝑒𝑑 𝑏𝑦 𝑠𝑜𝑙𝑣𝑒𝑛𝑡

1.7 1.5 5.2 0.7

Rf Ala = 8.8 = 𝟎. 𝟏𝟗 Rf Glu = 8.8 = 𝟎. 𝟏𝟕 Rf Val = 8.8 = 𝟎. 𝟓𝟗 Rf Lys = 8.8 = 𝟎. 𝟖

2.6 1.5 0
Rf Try = 8.8 = 𝟎. 𝟑𝟎 Rf Unknown = 8.8 = 𝟎. 𝟏𝟕 Rf Hydrol = 8.8 = 𝟎

Distance from origin to final solvent line 8.8 cm

Amino Acid Color Distance Traveled Rf

Alanine violet 1.7 0,19
Glutamic Acid violet 1.5 0.17
Valine violet 5.2 0.59
Lysine violet 0.7 0.08
Tyrosine light violet 2.6 0.30
Unknown violet 1.5 0.17
Hydrol white 0 0

Amino Acid in Unknown : Glutamic Acid

 A mixture of unknown amino acids can be separated and identified by means of paper
chromatography. The position of the amino acids in the chromatogram can be detected by spraying with
ninhydrin, which reacts with amino acids to yield highly coloured products (purple). The relationship
between the distance travelled by an amino acid and the distance travelled by the solvent was presented by
the Rf value. The unknown amino acid that was given to each group can be identify by matching the R f value
and the color with ninhydrin of the known amino acid. The unknown amino acid that was given to our
group was Glutamic Acid.

III. CONCLUSION
Thus, all amino acids have the alpha carbon bonded to a hydrogen atom, carboxyl group,
and amino group. The "R" group varies among amino acids and determines the differences between
these protein monomers. Amino acids are grouped according to polarities and pH: Group I:
Nonpolar amino acids; Group II: Polar, uncharged amino acids; & Group III: Acidic amino acids.
Group I amino acids are glycine, alanine, valine, leucine, isoleucine, proline, phenylalanine,
methionine, and tryptophan. The R groups of these amino acids have either aliphatic or aromatic
groups. This makes them hydrophobic (“water fearing”). Group II amino acids are serine, cysteine,
threonine, tyrosine, asparagine, and glutamine. The side chains in this group possess a spectrum of
functional groups. The two amino acids in this group are aspartic acid and glutamic acid. Each has a
carboxylic acid on its side chain that gives it acidic (proton-donating) properties.
In addition, in order to separate the amino acids in a given mixture, chromatography
technique was used.

IV. REFERENCE(S)
 https://courses.lumenlearning.com/introchem/chapter/amino-acids/
 http://hyperphysics.phy-astr.gsu.edu/hbase/Organic/aminostruct.html
 https://vlab.amrita.edu/?sub=3&brch=63&sim=154&cnt=1