CHAPTER 1

PREFACE

1.1 Background of The Problem

Amino acid is a carboxylic acid having an amino group. Amino acid
contained as a component of proteins having -NH2 at the carbon atom of the
position of the -COOH group. The types of amino acids, the sequence of the
amino acids are strung way, as well as the spatial relationship of amino acids
such asan determine the 3-dimensional structure and biological properties of
proteins is simple.
While the protein (the root word of the language Yunaniyang Protos means
"most important") adalahsenyawa high molecular weight organic compound
which is a monomer-monomerasam polimerdari aminoyang connected to each
other by peptide bonds. Protein molecules containing carbon, hydrogen,
oxygen, phosphorus sulfurserta nitrogendan sometimes. Protein plays an
important role in the structure and function of living organisms and viruses
semuasel.

1.2 Formulation of The Problem

1. whether the amino acid ?
2. whether the protein ?

1.3 Objective
1. To know and understand the amoni acid
2. To know and understand the protin

CHAPTER 2
LITERATURE REVIEW

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2.1 AMINO ACID
2.1.1 Definition of Amino Acid
Amino acids which are the monomers (building blocks) protein is a
compound having two functional groups are amino and carboxyl
groups. At the amino acids, the amino group attached to the carbon
adjacent to the carboxyl group (C-) or it can be said also that the
amine group and the carboxyl group of the amino acid bound to the
same carbon atoms.
The structure of the amino acids in general is one of the C atoms
that binds four groups: amine groups (NH2), carboxyl group (COOH),
hydrogen (H), and a leaving group (R, of residue) or also called group
or side chains distinguish one amino acid with another amino acid. The
central C atom called C atoms ("C-alpha") in accordance with the
naming bergugus carboxyl compounds, namely the C atom which is
attached directly to the carboxyl group. Therefore, the amine group is
also attached to this C atom, the compound is an -amino acid.
Amino acids are usually classified by the chemical nature of the side
chain into four groups. The side chain can make an amino acid is a
weak acid, weak base, if polar hydrophilic and hydrophobic if
nonpolar

2.1.2 Nomenclature of Amino Acids

In addition to the name of the amino acid bases, also diberika the
systematic chemical name (IUPAC). This time there are two systems
of nomenclature used for amino acids. First by naming the carbon
atom that binds carboxyl and amino as alpha. Further bonded carbon
(of the chain R) is called beta, gamma and so on.
This system is slowly pressed by the system by giving the number
of carbon atoms.
Table names and structures 20 kinds of amino acids making up the protein

n
o Nama biasa Nama sistematika
1 Alanin As. 2-amino propanoat

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2 Valin As. 2-amino-3-metil butanoat
3 Leusin As. 2-amino-4-metil pentanoat
4 Isoleusin As. 2-amino-4-metil pentanoat
5 Prolin As.2-amino-3 fenilpropanoat
6 Fenilalanin As. 2-amino-3 fenilpropanoat
7 Triptofan As. 2-amino-3 (3-idolil)-propanoat
8 Metionin As. 2-amino-4-(metal tin) butanoat
9 Glisin As. 2 amino etanoat
1
0 Serin As. 2-amino-3-hidroksil propaniat
11 Treonin As. 2-amino-3-hidroksin propaniat
1
2 Sistein As. 2-amino-3-merkapto propanoat
1
3 Tirosin As. 2-amino-3-(p-hidroksil fenil) propanoat
1
4 Asparagin As. 2-amino-suksinat
1
5 Glutamin As. 2 amino glutaramat
1
6 Asam aspartat As. 2-amino-suksinat
1
7 Asam glutamate As. 2-glutarat
1
8 Lisin As. 2,6-diamino-heksanoat
1
9 Arginin As. 2-amino-5-guanido valerat
2 Histidin As. 2-amino-3-imidazol propanoat

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0

Table names and abbreviations of the 20th amino acid

Singkatan (symbol)
No Nama biasa 3 huruf 1 huruf
1 Alanin Ala A
2 Valin Val V
3 Leusin Leu L
4 Isoleusin Ile I
5 Prolin Pro P
6 Fenilalanin Fen F
7 Triptofan Trp W
8 Metionin Met M
9 Glisin Gli G
10 Serin Ser S
11 Treonin Tre T
12 Sistein Sis C
13 Tirosin Tiv Y
14 Asparagin Asn N
15 Glutamin Gln G
16 Asam aspartat Asp D
17 Asam glutamat Glu E
18 Lisin Lis K

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19 Arginin Arg R
20 Histidin His H

2.1.3 Amino Acid Stereochemistry

All amino acids obtained from the hydrolysis of proteins, except
glycine have optically active properties which can rotate the plane of
polarization of light when examined with a polarimeter. Active optical
properties caused by the asymmetric carbon atom is an atom that is
bonded to four different groups. The amount of stereo isomers that
may occur equal to 2n. n is the number of asymmetric carbon atoms.
All common amino acid found in protein except glycine have an
asymmetric carbon atom, while tronina and isoleucine each have two
asymmetric carbon atoms.
Konfugurasi absolute amino acid structure of the active optical
isomers derived from the stereo structure of monosaccharide molecules
that have the smallest carbon atoms, namely glyceraldehyde which has
an asymmetric carbon atoms. By convention both stereo isomeric
forms are expressed with L and D (no relation to destrorotatory and
levorotatory).

2.1.4 Amino Acid Synthesis

Some amino acid synthesis is commonly known among other
things:
1. Amination a-halo acid (substitution)
A-halogen acid derived from halogenated carboxylic acids
(Hell-Volhard-Zelinsky), for example brominated propanoic acid.
Furthermore, a next-propionic acid is added to concentrated
ammonia solution obtained and stored at room temperature for 4
days. After that in uapkan until dried and extracted with hot
absolute ethanol to remove bromide. Amino acids obtained in the
form of white crystals.
2. Strecker synthesis

5
 This method is the hydrolysis of a-amino nitrile obtained by
reacting aldehydes with ammonia and cyanide. The reaction takes
place
3. Amen
Reduction of an a-keto acid with H2, Pd catalyst NH3dan will
generate resemit an amino acid (a mixture of R and S amino acids)

2.1.5 The Chemical Reaction of Amino Acids

1. Ninhydrin reagent
A color reaction which is used to identify amino acid.
Nindhidrin is a very strong oxidizing agent that can cause oxidative
decarboxylation of a-amino acid to produce CO2.NH2dan an
aldehyde with a carbon atom less than the parent amino acids.
Ninhydrin which reacts with the amino terduksi then separated to
form blue-violet complex that absorbs light with a maximum
wavelength of 570 nm.
2. Sanger reaction
Sanger reaction is a reaction between a-amino with 1-fluoro-
2,4-dinitrobenzen (FDNB). In an atmosphere of weak bases FDNB
react with a-amino acid derivative to form 2,4-dinitfenil called
DNP-amino acids. This reaction is used for the determination of
amino acid N-end of a peptide chain.
3. Edman reaction
This reaction is a reaction between a-amino phenyl derivative
of phenyl isothiocyanate produces thiocarbonyl.
4. Peptide
When the amino group and the hydroxyl group of amino acids
combine to form a peptide bond, an element of amino acid residues
called amino acids. A peptide consists of 2 or more amino acid
residues are joined by peptide bonds or said also that if proteins
only partially hydrolyzed, the polymers are less formed from
amino acids called peptides.
Simple peptides containing two, three, four, or more amino
acid residues, respectively referred dipeptda, tripeptide,
tetrapeptida and so on. When the peptide contains many bond (say

6
 over 10) amino acid residues, peptide called polypeptide, many or
all of the protein hormone is a polypeptide simple.
Many amino acids bonded via peptide bonds to form
polypeptide chain branched One unit of amino acids in the
polypeptide chain are called residuals. Polypeptide chain has a
direction because the constituent units having different ends which
-amino groups and carboxyl group-. Amino tip is placed at the
beginning of the polypeptide chain, means the sequence of amino
acids in the polypeptide chain written preceded by the amino-
terminal residues.

Every living cell contains protein. Protein organic compounds

essential for living organisms and the highest concentration in the
muscle tissue of animals. Protein is an essential life-sustaining
materials. Skin, bone, muscle, blood, hormones, enzymes and organs
are all made up of protein.
Essential amino acids are amino acids required by the creature as a
framework proteinatau hidupsebagai constituent molecules important.
He called essential for an organism species when these species need
but are not able to produce its own or always short amino acid in
question.
Non-essential amino acid produced by the body include:
1. Tyrosine; first found in the cheese. In humans, these amino acids
are not esencial, but pembentukanya use of raw materials by the
enzyme phenylalanine phehidroksilase. According to research
conducted by the research institute of Environmental Health USA
1988, tyrosine also serves sebagia stimulant and sedative drugs that
eektif to improve mental and physical performance under pressure,
with no side effects. Tyrosine is contained in chicken liver, cheese,
avocado, banana, yeast, fish and meat.
2. Cysteine; though not an essential amino acid cysteine content of the
atom is almost equal to methionine. Cysteine is also found in foods
such as chili, garlic, onions, broccoli, oat, and wheat bulis core.

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3. Serin; The first time in the isolation of a protein fiber silk in 1865.
4. Proline; known as the most important function in the protein
component.
5. Glycine; in umu, the protein itself does not contain a lot of glycine
(except in the collagen-containing glycine than two thirds of its
content). The human body produces glycine in sufficient quantities.
6. Glutamic acid; because glutamate ions which can stimulate some
type of nerve that exist in the human tongue, glutamate in use in the
flavor industry. Find in everyday life in the form of salt derivatives
are referred to as monosodium glutamate or MSG.
7. Aspartic acid; often called aspartate. Its function in plants partially
known neurotransmitters in the brain and muscle nerves. Aspartate
is also possible to play a role in resistance to fatigue.
8. Ariginin; although non-essential to humans and other mammals,
but ariginin can be said as a half-essential amino acid because its
production depends heavily on the level of development and health
conditions. In children, ariginin very important. The main source of
food ariginin found in livestock products such as meat, milk, eggs,
and various processed. While from plant products, ariginin found in
chocolate and peanut seeds.
9. Alanine; foodstuffs found in other forms such as meat, fish, milk,
eggs, and nuts.
10. Histidine; for humans, histidine is an essential amino acid for
children.
11. Glutamine; is an amino acid which is also known as acid glumatik.
This amino acid serves as fuel for the brain that controls excess
ammonia that is formed in the body as a result of biochemical
processes. Naturally, glutamine is found in wheat and soybeans.
12. Asparagine; needed by the nervous system to maintain equilibrium
and in need also in the transformation of the amino acid.
Asparagine is found also in the meat (all kinds of sources), eggs
and milk (as well as products turunanya).

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 Essential Amino acids that are not produced by the body, are as
follows:
1. Tryptop
2. han; an essential amino acid, is several sources get from
carbohydrates. Tryptophan is found in eggs, meat, skim milk,
bananas, milk, and cheese.
3. Threonine: found in foodstuffs such as milk, meat, fish and sesame
bici.
4. Methionine: is esencial. Therefore, it should be taken from food.
The main source of methionine hdala fruits, meat (chicken, beef,
fish, milk (whole milk, several kinds of cheese), saturan (spinach,
garlic, corn) and legumes (peas, pistacio, cashews, lentils , tofu and
tempe).
5. Lysine; contained in soy protein, bici legumes, and fish. Average
per day lysine requirements are 1-1.5 g.
6. Leucine; widely available in foods high in protein, such as meat,
milk, brown rice and soybeans. In the soy milk products also
contain leucine encountered many.
7. isoleucine;
8. Phenylalanine; an essential amino asm into raw materials for the
formation of catecholamines. This is known as catecholamines
alertness-enhancing essential for transmission of nerve impulses.
Fenilalamin found in chicken meat, sapai, fish, eggs, and soy.
9. Valin; contained in livestock products such as meat, telar, milk and
cheese. In addition, this essential amino acid found in bici-grain
containing oils such as groundnut, sesame, and gentil).

2.2 PROTEIN
2.2.1 Definition of Protein
Proteins are composed of amino acids, each of which is connected
by peptide bonds. Nonetheless, in the early formation of proteins are
composed of 20 amino acids known as essential amino acids or basic
amino acids or amino acids making up the protein (proteinogenik).
These amino acids encoded by the DNA / RNA as the genetic code.
Protein (protos root of the Greek word meaning "most important") is
organikkompleks high molecular weight compounds which are

9
 polymers of amino acid monomers linked together by peptide bonds.
Protein molecules containing carbon, hydrogen, oxygen, phosphorus
sulfurserta nitrogendan sometimes. Protein plays an important role in
the structure and function of all living selmakhluk and viruses.
Most enzimatau subunit protein is an enzyme. Other types of
proteins play a role in structural or mechanical functions, such as the
proteins that form the cytoskeleton rods and joints. Proteins involved
in the immune system (immune) as an antibody, the control system in
the form of the hormone, as the storage component (in seed) and also
in the transport of nutrients. As a source of nutrition, the protein acts as
a source of amino acids for organismeyang not be able to form the
amino acids (heterotrophic).
Protein is one of the giant biomolecules, in addition to
polysaccharides, lipids, and polynucleotides, which is the main
constituent of living beings. In addition, the protein is one of the most
widely studied molekulyang in biochemistry. Protein discovered by
Jns Jakob Berzelius in 1838.
Equal to the natural protein biosynthesis gene expression. The
genetic code carried DNAditranskripsimenjadi RNA, which acts as a
template for translasiyang done ribosomes. Until this stage, the protein
is still "raw", are composed of amino acids proteinogenik. Through
posttranslational mechanisms, forming protein which has the full
biological function.

2.2.2 Synthesis Protein

Protein obtain from our food. Protein in the digestive system would
be broken down into simpler peptidpeptid whose structure is composed
of amino acids. This is done with the help of enzymes. The human
body requires 9 amino acids. That is nine amino acids can not be
synthesized by the body essential, while some amino acids can be
synthesized alone or not essential by the body. Totaling 21 amino
acids. After absorption in the intestine will be given to blood. Blood
carries the amino acids to every cell of the body. Code for amino acids
can be synthesized olehDNA not essential. This is called the

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 DNAtranskripsi. Then mRNA transcription results in further process
diribosomatau endoplasmic reticulum, referred to as translation.

2.2.3 The Function of The Protein

1. The structural proteins (body builder): protein membrane or cell wall;
protective tissue such as skin, hair, feathers, scales, hooves, horns,
beak and so on, as well as the
2. connective tissue such as bone, tendons, joints, etc.
3. The membrane proteins: contained in the cell membrane
4. contractile proteins: contained in the muscle fibers
5. Protein transport: binding and transporting other molecules such as
hemoglobin that transports O2
6. Protein shield: the whole antibody and blood clotting agents such as
fibrinogen
7. Protein backup: liberate amino acids when necessary, eg casein (milk
protein) and ovalbumin (egg white)
8. hormone: regulate growth and metabolism
9. Enzymes: catalyze biochemical reactions

2.2.4 Peptide Bond

1. Peptide bond is: an amide bond that links two amino acids
2. Compounds that form a compound called peptides
3. Written peptide bond with an amino acid having free NH3 + group on
the left and amino acids with free CO- group on the right.

2.2.5 Structure of Protein

1. Primary Structure
The primary structure shows the number, type and sequence of amino
acids in the protein molecule
The bond between amino acids is a peptide bond
2. Secondary Structure
Heliks and folded sheet are two secondary structures commonly
found in proteins or protein segments
3. Tertiary Structure
Tertiary structure of the polypeptide shown a tendency to form folds
or rolls, and thereby forming more complex structure
strengthened by some bond between the R groups in the molecule
amino acids that make up proteins

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 Some genius such commitments include: electrostatic bonding,
hydrogen bonding, hydrophobic interactions between the chains to
nonpolar, dipole-dipole interactions, and the bond is a covalent bond
diulfida
Covering globular protein and fiber

CHAPTER III
CLOSE

3.1 Conclussion
Amino acids which are the monomers (building blocks) protein is a
compound having two functional groups are amino and carboxyl groups. At the
amino acids, the amino group attached to the carbon adjacent to the carboxyl
group (C-) or it can be said also that the amine group and the carboxyl group
of the amino acid bound to the same carbon atoms.
Proteins are composed of amino acids, each of which is connected by
peptide bonds. Nonetheless, in the early formation of proteins are composed of
20 amino acids known as essential amino acids or basic amino acids or amino
acids making up the protein (proteinogenik). These amino acids encoded by the
DNA / RNA as the genetic code. Protein (protos root of the Greek word
meaning "most important") is organikkompleks high molecular weight

12
 compounds which are polymers of amino acid monomers linked together by
peptide bonds. Protein molecules containing carbon, hydrogen, oxygen,
phosphorus sulfurserta nitrogendan sometimes. Protein plays an important role
in the structure and function of all living selmakhluk and viruses.

3.2 Suggestion
This paper still has various types of shortcomings by him that constructive
criticism is highly appreciated.

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