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Complete report of Organic Chemistry II Experiment with title “Amino

Acid and Protein” by:
name : Istikfariyani Mubin
id : 1613442008
group : V (FIVE)
class : ICP of Chemistry Education
after checked and consulted with assistant and assistant coordinator, this report
has been accepted.

Makassar, December 2017

Assistant Coordinator Assistant

Yudhi Priyatmo, S.Pd Yuli Astuti

ID. 1413440023

Known by,
Responsibility Lecturer

Dr. Netti Herawati, S.Pd., M.Si

ID. 19741027 200002 2 001
Amino Acid and Protein
Before the experiment, the apprentice must understand the structure of
protein. During the experiment is expected to:
1. Can prove the existence of a peptide bond.
2. Can understand xantoproteat reaction and biuret test of the various various
contets of protein.
3. Understand about solubility and amphoteric properties of amino acids.
4. Skill to separated amino acid by paper chromatography and its identificatiom.
Proteins are composed of molecular building blocks called amino acids.
However, there are only 20 different amino acids present in human proteins.
Every amino acid consists of a central carbon atom called the -carbon bonded to
two functional groups: an amino group and a carboxylic acid group The -carbon is
also bonded to a hydrogen atom and an R group. It is the R group, which differs in
each of the 20 amino acids, that provides unique characteristics to each type of
amino acid. For example, alanine has a methyl, ¬CH3, as its R group

(Timberlake, 2012: 559).

Because amino acids contain both basic amino and acidic carboxyl groups,
they undergo an intramolecular acid–base reaction and exist in aqueous solution
primarily in the form of dipolar ions, called zwitterions (from the German zwitter,
meaning “hybrid”).

(uncharged) (switterion) (McMurry, 2011: 504).

Although we have drawn an amino
acid with uncharged amino ( and carboxylic
acid ( groups, these groups are ionized for
amino acids in most body fluids. At
physiological pH, the group gains to give its
ionized form and the ¬COOH group loses H+
to give its ionized form ¬COO-. An ionized
amino acid, which has both a positive charge
and a negative charge, is a dipolar ion called a
zwitterion. In the zwitterion, the ionized
regions have charge balance, which means that
the ionized amino acid has an overall zero charge. As zwitterions, amino acids are
similar to salts. Thus, amino acids have high melting points and are soluble in
water, but not in organic solvents (Timberlake, 2012: 560).
In addition, amino acids are amphiprotic, meaning that they can react
either as acids or as bases, depending on the circumstances. In aqueous acid
solution, an amino acid zwitterion is a base that accepts a proton onto its _ CO2_
group to yield a cation; in aqueous base solution, the zwitterion is an acid that
loses a proton from its _ NH3_ group to form an anion. The structures,
abbreviations (both one-letter and three-letter), and pKa values of the 20 amino
acids commonly found in proteins (McMurry, 2011: 504-505).
All the -amino acids except for glycine are chiral because the -carbon is
attached to four different atoms. Thus amino acids can exist as D and L isomers.
We can draw Fischer projections for -amino acids as we did in Chapter 12 for
aldehydes by placing the carboxylate group at the top and the R group at the
bottom. In the L isomer, the is on the left, and in the D isomer, it is on the right. In
biological systems, the only amino acids incorporated into proteins are the L
isomers. There are D amino acids found in nature, but not in proteins. Let’s take a
look at the isomers for L- and D-glyceraldehyde and the isomers of L- and D-
alanine and L- and D-cysteine (Timberlake, 2012: 560).
The concentrations of essential amino acids composition recovered in
human, camel, cow, goat and sheep milks. Phenylalanine was the major of the
essential amino acids in five species. Goat milk was characterized by low content
of methionine and high content of Threonine. Human, sheep, goat, camel and cow
milk are very rich in all essential amino acids except methionine. Glutamic acid
was the major of non-essential amino acid in five species. Human, cow and sheep
milk is characterized by low content of Arginine. In addition the five milk
samples are characterized by low content of Cystine. The branched chain of amino
acids in human, camel, cow, goat and sheep are presented in Table-3. Human,
camel, cow, goat and sheep milk are characterized by high content of leucine,
isoleucine and valine except milk of goat has low content in isoleucine. This
results are in agreement with findings that reported by Posati and Orr (1976).
However, several differences were found in essential, non- essential and branched
chain of amino acids patterns of five milks at p≤0.05 (Sabahelkheir, 2012: 32-33).
Ionic bonding is possible between a molecule containing an ammonium
ion and a molecule containing a carboxylate ion. Some important naturally
occurring molecules contain both groups – the amino acids. Both these functional
groups are ionized to form a structure known as a zwitterion (a neutral molecule
bearing both a positive and a negative charge) and intermolecular ionic bonding
can take place

(Patrick, 2003: 31).

According to Nelson (2004: 75), all 20 of the common amino acids are _-
amino acids. They have a carboxyl group and an amino group bonded to the same
carbon atom (the _ carbon) (Fig. 3–2). They differ from each other in their side
chains, or R groups, which vary in structure, size, and electric charge, and which
influence the solubility of the amino acids in water. In addition to these 20 amino
acids there are many less common ones. Some are residues modified after a
protein has been synthesized; others are amino acids present in living organisms
but not as constituents of proteins.
FIGURE 3–2 General structure of an amino acid. This structure is common to all but one of the
_-amino acids. (Proline, a cyclic amino acid, is the exception.) The R group or side chain (red)
attached to the _ carbon (blue) is different in each amino acid.

In addition to the 20 amino acids commonly found in proteins, 2 others—

selenocysteine and pyrrolysine—are found in some organisms, and more than 700
nonprotein amino acids are also found in nature. _-Aminobutyric acid (GABA),
for instance, is found in the brain and acts as a neurotransmitter; homocysteine is
found in blood and is linked to coronary heart disease; and thyroxine is found in
the thyroid gland, where it acts as a hormone

(McMurry, 2011:
Tyrosine Aspartic acid 505-507).
Phenylalanine, tyrosine, and tryptophan, with their aromatic side chains,
are relatively nonpolar (hydrophobic). All can participate in hydrophobic
interactions. The hydroxyl group of tyrosine can form hydrogen bonds, and it is
an important functional group in some enzymes. Tyrosine and tryptophan are
significantly more polar than phenylalanine, because of the tyrosine hydroxyl
group and the nitrogen of the tryptophan indole ring. (Nelson, 2004: 75).
A peptide bond is an amide bond that forms when the of one amino acid
reacts with the of the next amino acid. The linking of two or more amino acids by
peptide bonds forms a peptide. A chain of five amino acids is a pentapeptide, and
long chains of amino acids are called polypeptides. The dipeptide forms when the
carbonyl group in glycine bonds to the N atom in of alanine. During the
amidation, the O atom removed from the carboxylate combines with two H atoms
from ¬NH3 to produce H2O

(Timberlake, 2012: 566).

1. Apparatus
a. Test tube 14 pieces
b. Beaker glass 800 mL 1 piece
c. Beaker glass 50 mL 1 piece
d. Graduated cylinder 25 mL 2 pieces
e. Funnel 1 piece
f. Analytical balance 1 piece
g. Thermometer 110oC 1 piece
h. Watch glass 1 piece
i. Spray bottle 1 piece
j. Test tube rack 2 pieces
k. Drop pipette 3 pieces
l. Erlenmeyer 250 mL 1 piece
m. Wood clamp 2 pieces
n. Stir bar 1 piece
o. Spatula 1 piece
p. Tripod 1 piece
q. Wire gauze 1 piece
r. Spiritus burner 1 piece
s. Stopwatch 1 piece
t. Rough and smooth rag @ 1 piece
2. Chemical
a. L-tyrosine C9H11NO3
b. Glycine C2H5NO2
c. Aspartic acid C4H7NO4
d. Casein C18H22O6N
e. Hydrochloric acid 10% and 20% HCl
f. Urea CO(NH2)2
g. Sodium hydroxide 10% NaOH
h. Sodium nitrite solution 5% NaNO2
i. Copper (II) sulfate 2% CuSO4
j. Nitric acid HNO3
k. Aquades H2O (l)
l. Litmus paper
m. Aluminum foil
n. Filter paper
o. Ice H2O (s)
p. Hot water H2O (l)
q. Matches
1. Solubility and Amphoteric Properties
a. 0,1 gr of glycine crystal, aspartic acid crystal, and L-tyrosine crystal was
b. The crystal was put into different test tube.
c. Crystal of glycine was put in 1st test tube.
d. Aspartic acid crystal was put in 2nd test tube.
e. L-tyrosine crystal was put in 3rd test tube.
f. Each test tube was added with 2 mL of H2O.
g. the acidity of each test tube was tested.
h. 0,1 gr of L-tyrosine was weighed.
i. The crystal was put in test tube.
j. 2 mL of H2O was added into the test tube.
k. 1 mL of NaOH 10% was added too.
l. A few drops of HCl 10% also was added into the solution until the solution is
m. The solution was shaken and observed with litmus paper.
n. 10 drops of HCl 10% was added again into the solution.
o. 0,1 gr of casein was weighed
p. The crystal was put in test tube.
q. 5 mL of H2O was added into test tube too.
r. The solution was added with 2 mL of NaOH 10%.
s. The solution was shaken until it was formed colloid.
t. 4 mL of this solution was saved for the next experiment.
2. Reaction with Nitric Acid (HNO3)
a. 0,1 gr of glycine was weighed.
b. It was put in 1st test tube.
c. 5 mL of HCl 10% was added in test tube.
d. 5 mL of HCl 10% was filled in another test tube or 2nd test tube as a
e. The both of test tube was cooled until the temperature was 0oC.
f. 1 mL of NaNO2 5% was added into each test tube.
g. 2 mL casein solution that we had saved was cooled.
h. 1 mL of NaNO2 5% was added too.
3. Biuret Test
a. 0,5 gr of urea was weighted.
b. It was heated until it was melted and gas was formed.
c. The acidity of gas urea was tested with litmus paper and the smell of gas was
smelled out.
d. Then urea was heated again until without gas formed again and urea was
e. Urea was cooled and was dissolved with hot water.
f. It was filtered with filter paper.
g. The filtrate was added with 2 mL of NaOH 10%.
h. 2-3 drops of CuSO4 2% was added in filtrate of urea.
i. The solution was shaken.
j. The color was observed.
k. 0,5 gr of urea was weighted as a comparator solution.
l. 3 mL of H2O was added with urea.
m. 2 mL of NaOH 10% and 2-3 drops of CuSO4 2% was added too.
n. The solution was compared with the result of experiment before.
o. 2 mL of casein from experiment before was added with 2 mL of H2O.
p. It was added with 2-3 drops of CuSO4 2%.
q. The solution was shaken and observed.
4. Xanthoproteic Test
a. 0,1 gr of casein was weighted.
b. It was added with 2 mL of HNO3.
c. It was heated carefully.
d. Solution of NaOH 10% was added to neutralize.
e. It was added a little more base again.
5. Hydrolysis of Protein
a. 0,5 gr of casein was weighted.
b. It was added with 10 mL of HCl 20%.
c. It was heated during 30 minutes.
d. It was cooled until the temperature same with room temperature
e. Take 5 mL of hydrolysis result and it was cooled in ice.
f. 5 mL of other hydrolysis result was added with 3 mL of NaOH 10% and 2
drops of CuSO4 2%.
g. It was heated.
h. The solution was compared.
1. Solubility and Amphoteric Properties
No. Activities Result
Crystal of glycine + 2 mL of H2O Soluble, the color is colorless
and there is sediment.
Red litmus paper test Base

L- aspartate acid + 2 mL of H2O Not soluble, colorless, and

there is sediment
Red litmus paper test Acid

L-tyrosine + 2 mL of H2O Soluble, the color of solution is

white, and there is no
Red litmus paper test Base
L-tyrosine + 2 mL of H2O + 1 mL Turbid into solution
2 of NaOH 10%
Litmus paper test (blue) Base (blue)
+HCl 10% until the solution is acid Acid (red) and there is
+ 10 drops of HCl 10% sediment.
0,1 gr of casein + 5 mL of H2O + 2 The solution formed colloid.
mL of NaOH 10%
2. Reaction with Nitric Acid (HNO3)
No. Activities Result
0,1 gr of glycine + 5 mL of HCl Soluble and the color is turbid.
10% and it cool until the
temperature is 0oC Turbid and there are many
+ 1 mL of NaNO2 5% bubbles.
(Comparator) Colorless
5 mL of HCl 10% Colorless
Cooled Colorless and there are a little
+ 1 mL of NaNO2 5% bubbles.
2 mL of casein Turbid solution
Cooled Turbid solution
+ 1 mL of NaNO2 5% Turbid solution and there is
yellow sediment formed.
3. Biuret Test
No. Activities Result
0,5 gr of urea heat until it melts Urea melts, there is gas
formed, and the smell is rancid.
Acidity test Base (red litmus paper become
blue litmus paper).
Heat again Urea become a solid.
Dissolve with hot water Colorless.
Filtering Colorless.
+ 2 mL of NaOH 10% + 3 drops of Soluble and the color is purple.
CuSO4 2%
0,5 gr of urea + 3 mL of H2O + 2 Colorless become blue
mL of NaOH 10% + 3 drops of solution.
CuSO4 2%
2 mL of casein + 2 mL of H2O Colorless.
2 + 3 drops of CuSO4 2% Blue solution and formed
4. Xanthoproteic Test
No. Activities Result
0,1 gr of casein + 2 mL of HNO3 The color of solution is yellow.

Heated The color become light yellow

Cooled the solution + NaOH 10% The color become yellow.

5. Hydrolysis of Protein
No. Activities Result
0,5 gr of casein + 10 mL of HCl 20% The color of solution is
Heated until 30 minutes The color become dark
Cooled it until temperature room brown.
1st test tube: The color is dark brown
5 mL of solution and cooled in ice
2nd test tube: The color is dark brown.
1 5 mL of solution + 3 mL of NaOH
10% and heated The solution formed two
Upper layer: White
+ 3 drops of CuSO4 2% Bottom layer: Light brown
Brown solution
1. Kelarutan dan sifat amfoterik
Tujuan dilakukan percobaan ini yaitu untuk mengetahui kelarutan dan sifat
amfoterik dari asam-asam amino. Dalam pengujian ini digunakan tiga jenis
larutan uji, diantaranya glisin, L-tirosin, dan kasein.
Pada pengujian glisin, menunjukkan bahwa glisin dapat larut sempurna
dalam air. Hal ini disebabkan karena kebebasan gugus amin lebih besar dari pada
karboksil, maka kedua gugus amin dan karboksil di dalam asam amino akan
saling bereaksi menghasilkan ion zwitter. Oleh karena itu struktur dipolar ini
maka asam amino mudah larut dalam air. Glisin diuji dengan menggunakan kertas
lakmus merah yang kemudian berubah warna menjadi biru sebagai penanda
bahwa glisin bersifat basa seingga hasil percobaan yang dilakukan tidak sesuai
dengan teori.
H – C – COOH + H2O → H – CH – COO- + H2O
NH2 NH3+
( gilisin ) ( ion dipolar )
Apabila dilihat dari strukturnya seharusnya glisin bersifat netral karena ia tidak
mengandung gugus karbonil dan gugus amina yang berlebih.
Pada pengujian L-tirosin, menunjukkan bahwa ia larut dalam air kerena
adanya ion H+ yang terdisosiasi dalam larutan yang berasal dari gugus karboksil ..
Sedangkan pada pengujian pH menunjukkan L-tirosin bersifat basa. Hal ini tidak
sesuai dengan teori dimana L-tirosin bersifat netral. Dimana reaksinya yaitu :


NH3 NH2+
( L-Tirosin )
Dengan menggunakan bahan uji L-aspartat menunjukkan bahwa asam
amino ini tidak larut dalam air, ini disebabkan karena R asam aspartat
mengandung C sehingga hanya sebagian yang bisa larut. Sedangkan pada
pengujian pH, menunjukkan ia bersifat asam. Hal ini membuktikan bahwa L-
aspartat merupakan asam amino yang apabila direaksikan dengan air, rantai
karboksil pada rantai sampingnya akan melepaskan proton ke air sehingga
terbentuk 2 muatan negatif dan 1 muatan positif. Reaksinya :
HOOC – CH – CH2 – COOH + H2O → - OOC – CH – CH2 – COO - + H3O+
NH2+ NH3+
Percobaan L-tirosin yang ditambahkan dengan NaOH 10 % menyebabkan
pHnya menjadi basa. Setelh itu ditetesi dengan HCl sehingga ia bersifat asam. Hal
ini menunjukkan bahwa L-tirosin bersifat amfoterik karena dapat bereaksi dengan
asam maupun basa.
Reaksi dengan NaOH:
NH3+ NH2
( L-Tyrosine witterion ) ( L-Tyrosine pH>6 )
+ 2H2O
Reaksi dengan HCl:
+ Cl- + NaOH + H2O
Pada pengujian kasein menunjukkan bahwa ia sukar larut dalam air
sehingga terbentuk koloid. Hal ini dikarenakan struktur kasein yang mengandung
rantai benzene, selain itu kasein merupakan jenis protein politirosin dengan jenis
atom karbon panjang yang menandakan bahwa terdapat gugus benzena dengan
kestabilan yang tinggi di dalamnya.
Pada percobaan ini, kasein yang ditambahkan dengan air lalu ditambah
dengan NaOH berfungsi untuk membasakan larutan terbentuk koloid yang
menunjukkan bahwa kasein bereaksi dengan basa. Reaksinya :
-NH – CH – C – N – CH – C – -NH – C – COOH
+ H2O

2. Reaksi dengan asam nitrit
Percobaan ini bertujuan untuk mendeteksi adanya gugus amin. Pada saat
glisin dereaksikan dengan HCl untuk memberikan suasana asam, lalu
ditambahkan lagi dengan NaNO2 yang mampu bereaksi dengan asam amino gas
N2 setelah itu didinginkan untuk mempercepat reaksi dan menghasilkan larutan
keruh dan terdapat banyak gelembung gas. Hal ini menunjukkan bahwa asam
amino ini mengandung gugus amin yang bereaksi dnegan nitrit (HNO2)
menghasilkan gas N2. Reaksinya :
H – CH – COOH + HCl + NaNO2 → H – CH – COOH + H2O + N2 +NaCl
Sedangakan pada larutan tanpa glisin yaitu campuran HCl dan NaNO2
menghasilkan larutan bening dan terdapat sedikit gelembung, seharusnya pada
percobaan ini menghasilkan gas NO. reaksinya :
HCl + NaNO2 → HNO2 + NaCl
3HNO3 ⇄ H+ + NO3- + H2O + 2NO
Sedangkan untuk larutan uji kasein yang ditambahkan dengan NaNO2
menghasilkan larutan keruh, terdapat endapan berwarna kuning dan larutan tanpa
gelembung. Hal ini menunjukkan tidak terdapat gugus amin yang bebas sehingga
tidak terbentuk gas N2. Reaksinya:
-NH – CH – C – N – CH – C – + NaNO2 nH2N – CH – COONa + HNO3

( kasein ) ( natrium nitrit)
3. Uji Biuret
Percobaan ini bertujuan untuk menguji ikatan peptide dalam protein. Hal
ini ditandai dengan terbentuknya larutan berwarna ungu. Urea yang dilelehkan
untuk menghasilkan gas NH3 kemudian diukur pH nya dengan menggunakan
kertas lakmus merah yang berubah warna menajadi biru sebagai penanda bahwa
urea bersifat basa. Urea tersebut dipanaskan kemudian dicuci dengan
menggunakan air panas sehingga larutan tidak berwarna. Pada penambahan
NaOH dan CuSO4 urea larut dan warna berubah menjadi ungu. Penambahan
NaOH bertujuan untuk memberikan situasi alkalin sehinggal larutan dapat
terbentuk dan berubah warna sehingga mencegah deposisi dari Cu(OH)2. Fungsi
penambahan CuSO4 yakni mematahkan ikatan peptida. Hal ini menunjukkan
bahwa pada kasein terdapat ikatan peptide. Reaksi pemanasan urea adalah
H2N – C – NH2 + H2N – C – NH2 → H2N – C – NH – C – NH2 + NH3
( urea )
H2N – C – NH – C – NH2 + CuSO4 → H2N H2N
NH Cu2+ NH
(tembaga NH3
( urea ) sulfat) Senyawa kompleks
Sebagai pembanding, larutan urea ditambahkan dengan NaOH dan
direaksikan dengan CuSO4 menghasilkan larutan biru prusi yang berarti tidak
terdapat ikatan peptida.
Kasein yang direaksikan dengan aquades dan larutan CuSO4 menghsilkan
larutan ungu yang berarti terdapat ikatan peptida kerena kasein adalah protein
yang tersusun dari asam amino.
4. Uji Xantroproteat
Percobaan ini bertujuan untuk membuktikan adanya cincin aromatik. Pada
percobaan ini kasein dilarutkan dengan asam nitrat pekat dan menghasilkan
larutan kuning. Kasein digunakan dalam hal ini karena ia dapat dengan mudah
dipisahkan dari campurannya. Setelah itu larutan dipanaskan dan ditambahkna
dengan NaOH 10 % menghasilkan larutan kuning, tetapi setelah ditambahkan
basa berlebih larutan berubah menjadi warna kning pucat. Hal ini menunjukkan
adanya cincin aromatik pada kasein yang mengalami nitrasi pada saat
penambahan asam nitrat sehingga menghsilkan nitro yang berwarna kuning. Ini
sesuai dengan teori dimana adanya cincin aromatik pada kasen ditandai dengan
perubahan warna larutan menjadi kuning.
H2N – CH – C – NH – CH – C + NHO3

( kasein ) (asam nitrat)
H2N – CH – C – NH – CH – C – OH
H2N – CH – C – NH – CH – C – OH + NaOH
H2N – CH – C – NH – CH – C – OH + NaOH
5. Hidrolisis Protein
Percobaan ini bertujuan untuk memutuskan ikatan peptida. Pada
percobaan ini kasein dilarutkan dalam HCl menghasilkan larutan bening yang
berarti larutan larut sempurna. Setelah itu larutan dipanaskan yang bertujuan
untuk mempercepat reaksi hidrolisis. Larutan kemudian dibagi menjadi dua dalam
tabung reaksi yang berbeda, pada tabung reaksi pertama larutan didinginkan dan
diperoleh larutan berwarna coklat yang yang berarti kasein telah terhidrolisis
menjadi asam-asam aminonya sebab hidrolisis menyebabkan putusnya ikatan
peptida protein.
Larutan pada tabung reaksi kedua didinginkan ditambah dengan NaOH
menghasilkan dua lapisan yakni pada lapisan atas berwarna putih yang merupakan
sisa HCl dan NaOH sedangkan pada lapisan bawah berwarna coklat yang
merupakan kasein yang telah terputus ikatan peptidanya. Dan pada pengujian
dengan CuSO4 menghasilkan larutan berwarna coklat. Hal ini membuktikan pada
proses hidrolisis, ikatan peptidanya terputus sehingga pada saat penambahan
CuSO4 manghasilkan pengujian yang positif. Reaksinya :

-NH – CH – C – N – CH – C – O
CH2 O H CH2 O HCl nH2N – OH – C – OH

n OH
+ H2O
H2N – Cu – C – OH + NaOH H2N – CH – C – ONa + H2O
H2N – Cu – C – Ona + CuSO4 + 2H2O H2N – CH – C – ONa + H2O +
Cu(OH)2 + H2SO4
1. Conclusion
a. The existance of peptide bond can proved by biuret test marked with color
changing became purple.
b. Xanthoproteic test shown benzene group in amino acid that marked by color
changing became yellow cause nitration reaction in benzene group when
addition of HNO3. Biurette test shown the present of peptide bond in protein
that marked by color changing became purple cause ion Cu2+ react with biuret
in alkaline solution.
c. Amino acid soluble in water because it has dipolar structure. Amino acid are
amphoteric which reacts alkaline and acid because R group –NH2 and –COOH
are free.
d. To identificate the free amine group can react with HNO3 that marked the
present of gases bubbles (N2).Protein can hydrolysis became amino acid by
termination of peptide bond.
2. Suggestion
a. I suggest to apprentice should be carefully and focus in laboratiory so we can
got the result which accordance with theory.
b. I suggest to assistant for more care with us when do the experiment so there is
no incident in the laboratory.

McMurry, John. 2011. Fundamental of Organic Chemistry Seventh Edition. USA:

Brooks / Cole Cengange Learning.
Nelson, David L. 2004. Lehninger Principles of Biochemistry Fourth EditionI.
Canada: W. H. Freeman.
Patrick, Graham L. 2003. Organic Chemistry Second Edition. USA: Fulfilment
Sabahelkheir, MK, et al. 2012. Amino Acid Composition of Human and Animal’s
Milk ( Camel, Cow, Sheep and Goat ). ARPN Journal of Science and
Technology. Vol 2, Issue 2, Pages 3.
Timberlake, Karen C. 2012. Chemistry an Introduction to General, Organic and
Biological Chemistry Eleventh Edition. USA: Pearson education, Inc.

1. Giv the molecular formula of glycine, tyrosine and explain about acidic,
alkaline and neutral if solution in the water.
a. Glycine : CH2 – COOH
Glycine is neutral amino acid because not have amino or carboxylic group in
the side chain (R) or in the structure.
b. Aspartate Acid : COOH – CH2 – CH – COOH
Aspartic acid is acidic amino acid because have carboxylic group in the side
chain. This carboxylic acid will lose its proton in the water so form aspartate
HOOC – CH2 – CH – COOH + H2O -
OOC – CH2 – CH – COO- + H2O
NH2 NH3+
( Aspartate Acid ) ( Aspartate Ion )
c. Tyrosine :


Tyrosine is neutral amino acid because not have amine group and carboxylic
group in its shok chain (R).
2. Write the reaction that explain what have if the alkaline solution is
neutralization with acidic solution.
a. Alkaline solution of base
NaOH + HCl NaCl + H2O
b. Alkaline solution of acid
KCl + H2SO4 K2SO4 + HCl
This reaction, acid alkaline solution produce salt and acid.
3. Explain the different of casein properties and of hydrolysis result to nitrite
acid and biuret test.
a. The casein reacts with itrict acid accur hydrolysis of the protein polumers.
This hydrolysis produces amino acid monomers in which a peptide bond is
formed until there is no longer a free amine group of the casein, this reaction
form N2 gasses.
b. To biuret test, casein is still in the form of protein because there is a clutser of
peptides (COO-NH) and a colour reaction common to the peptides that is
charactterized by the formation of a purple color. This occurs because the
color reaction compound formed between the Cu2+ complexes with N of the
peptide molecule.
4. Suggest explanation of “aspartic acid will move slower than phenylanine”, on
the paper chromatography experiment.
In the experiment paper chromatography, aspartic acid will move faster
than phenylalanine because aspartic has a molecular size smaller than he size
of molecules of phenilalanine, so aspartic acid is early to absorbed by the
pores of the filter paper.