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Amino Acids and

Proteins
Larry Scheffler
Lincoln High
School
Portland OR

Amino Acids
Amino acids have both
a carboxyl group
-COOH
an amino group
-NH2
in the same
molecule..

Amino Acid
Structure
The general formula of an amino acid
is shown here
The group designated by R is usually
a carbon chain but other
structures are also
possible
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Amino Acid Structure


Amino acids may be
characterized as , ,
or amino acids
depending on the
location of the amino
group in the carbon
chain.
are on the carbon
adjacent to the
carboxyl group.
are on the 2nd
carbon
on the 3rd carbon
from the carboxyl

Amino Acids Proteins


Amino acids are the building

blocks of proteins. Proteins are


natural polymers of successive
amino acids
There are 20 different amino
acids that make up human
proteins

amino acids
Amino acids found
in proteins are
amino acids.
The amino group
is always found on
the carbon
adjacent to the
carboxyl group
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Amino Acid
Functions

1.

2.

Amino acids are the building blocks


of proteins
Some amino acids and their
derivatives function as
neurotransmitters and other
regulators
Examples Include
L-dopamine
Epinephrine
Thyroxine
Histidine

Amino Acids and Proteins


Amino acids
forming
proteins may
be
characterized
as Acidic,
Basic, or
neutral
depending on
the character
of the side
chain
attached.

Acidic Amino Acids


There are
two acidic
amino
acids.
There are
two
carboxyl
groups and
only one
amino

(asp)

(glu)
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Basic Amino Acids I


These amino
acids are
basic. They
have more
amino
groups than
carboxyl
groups
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Basic Amino Acids II


These amino
acids are
also basic.
They have
more amino
groups than
carboxyl
groups
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Neutral Amino Acids


I
These amino
Acids are
considered
neutral. There
is one
carboxyl
group per
amino group

(ala)

(gly)

((leu

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Neutral Amino Acids


II
(Ser)
(Tyr)

(Val)
(Trp)

(Cys)

(Met)

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Neutral Amino Acids


III
(Ile)

(Thr)

(Asp)
(Phe)

(Gln)

(Pro)

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Amino Acids and


Optical Isomers

Except for glycine, all amino acids


have a chiral carbon atom. Therefore
they can have optical isomers
The amino acids found in proteins are
all levarotatory or L forms.

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Amino Acids are


Amphoteric
Amino acids are amphoteric. They are capable of

behaving as both an acid and a base, since they have


both a proton donor group and a proton acceptor
group.

In neutral aqueous solutions the proton typically


migrates from the carboxyl group to the amino group,
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leaving an ion with both a (+) and a (-) charge.

The Zwitterion
This dipolar ion form is known as a
Zwitterion.

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Essential Amino Acids

Of the 20 amino acids that make


up proteins 10 of them can be
synthesized by the human body
The other 10 amino acids must be
acquired from food sources.
These amino acids are known as
essential amino acids
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Essential Amino Acids

Essential amino acidsNon-Essential amino acids


Arginine
Alanine (from pyruvic acid)
Histidine
Asparagine (from aspartic acid)
Isoleucine
Aspartic Acid (from oxaloacetic acid)
Leucine
Cysteine
Lysine
Glutamic Acid (from oxoglutaric acid)
Methionine
Glutamine (from glutamic acid)
Phenylalanine
Glycine (from serine and threonine)
Threonine
Proline (from glutamic acid)
Tryptophan
Serine (from glucose)
Valine
Tyrosine (from phenylalanine)
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Essential Amino Acids


Complete protein

Contains all 10
essential amino acids
Proteins derived from
animal sources are
complete proteins
Beans contain some
complete protein as
well

Incomplete protein

Lack one of more of the


essential amino acids
Most vegetable proteins
are incomplete proteins
Beans are an exception
to this generalizations

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Peptide Bond
When two amino acids combine,
there is a formation of an amide
and a loss of a water molecule

+ H2O
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Proteins- Levels of
Structure
Amino acids can undergo condensation
reactions in any order, thus making it
possible to form large numbers of
proteins.
Structurally, proteins can be described in
four ways.
1. Primary
2. Secondary
3. Tertiary
4. Quaternary structure.

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Primary Structure
The primary structure of a protein is
defined by the sequence of amino acids,
which form the protein. This sequence is
determined by the base pair sequence in
the DNA used to create it. The sequence for
bovine insulin is shown below

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Secondary Structure

The secondary structure describes the way


that the chain of amino acids folds itself due
to intramolecular hydrogen bonding
Two common secondary structures are
the Helix

and the sheet

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Tertiary Structure

The tertiary structure


maintains the three
dimensional shape of
the protein.

The amino acid chain


(in the helical, pleated
or random coil form)
links itself in places to
form the unique twisted
or folded shape of the
protein.
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Tertiary Structure

There are four ways in which parts of the amino acid


chains interact to stabilize its tertiary shape.. They include:

I.--

Covalent bonding, for


example disulfide bridges
formed when two cysteine
molecules combine in which
the SH groups are oxidized:
II.-- Hydrogen bonding between
polar groups on the side chain.
III.-- Salt bridges (ionic bonds)
formed between NH2 and
COOH groups
IV.-- Hydrophobic interactions.

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Quaternary
Structure
Many
proteins are not single strands
The diagram below shows the quaternary
structure of an enzyme having four interwoven
amino acid strands

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Denaturing Proteins

The natural or native structures of


proteins may be altered, and their
biological activity changed or
destroyed by treatment that does not
disrupt the primary structure.
Following denaturation, some
proteins will return to their native
structures under proper conditions;
but extreme conditions, such as
strong heating, usually cause
irreversible change.
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Denaturing Proteins

Heat

Ultraviolet
Radiation

Strong Acids
or Bases

Urea

Some Organic
Solvents

Agitation

hydrogen bonds are broken by increased


translational
and vibrational energy.(coagulation of egg white
albumin on frying.)
Similar to heat
(sunburn)
salt formation; disruption of hydrogen bonds.
(skin blisters and burns, protein precipitation.)
competition for hydrogen bonds.
(precipitation of soluble proteins.)
(e.g. ethanol & acetone) change in dielectric
constant and hydration of ionic groups.
(disinfectant action and precipitation of protein.)
shearing of hydrogen bonds.

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Sickle Cell Anemia

A small change in
the sequence of
the primary
structure can
have a significant
impact on protein
structure
In sickle cell
anemia a
glutamic acid is
replaced by a
valine in the
amino acid
sequence
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Ninhydrin Reaction

Triketohydrindene hydrate, commonly known


as ninhydrin, reacts with amino acids to form
a purple colored imino derivative, This
derivative forms a useful test for amino
acids, most of which are colorless.

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Protein Tests: Biuret

Biuret reagent is a light blue


solution containing Cu2+ ion
in an alkaline solution.
Biuret turns purple when
mixed with a solution
containing protein. The
purple color is formed when
copper ions in the biuret
reagent react with the
peptide bonds of the
polypeptide chains to form a
complex.
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Xanthroprotic Test

Concentrated Nitric acid will form a yellow


complex with tryptophan and Tyrosine side
chains in proteins

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Disulfide Bridge Test

Disulfide bridges will react with


Pb2+ ion from lead acetate in an
acidfied solution. A black
precipitate indicates the presence
of disulfide-bonded cysteine in
proteins.

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