Amino Acids and Proteins

Amino Acids
Amino acids have
both

a carboxyl group
-COOH

an amino group
-NH2
in the same
molecule..
2

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

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 group
4

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

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:
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 group per
molecule

(asp)

(glu)
9

Basic Amino Acids

These amino
acids are
basic. They
have more
amino
groups than
carboxyl
groups
10

Basic Amino Acids

These amino
acids are
also basic.
They have
more amino
groups than
carboxyl
groups
11

Neutral Amino Acids

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

(ala)

(gly)

12

Neutral Amino Acids

(Ser)
(Tyr)

(Val)
(Trp)

(Cys)

(Met)

13

Neutral Amino Acids

(Ile)

(Thr)

(Asp)

(Gln)
14

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.

16

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,
leaving an ion with both a (+) and a (-) charge.

17

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

18

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

19

Essential Amino Acids

Essential amino acids
Arginine
Histidine
Isoleucine
Leucine

Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine

Non-Essential amino acids

Alanine (from pyruvic acid)
Asparagine (from aspartic acid)
Aspartic Acid (from oxaloacetic acid)
Cysteine
Glutamic Acid (from oxoglutaric acid)
Glutamine (from glutamic acid)
Glycine (from serine and threonine)
Proline (from glutamic acid)
Serine (from glucose)
Tyrosine (from phenylalanine)
20

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

21

Essential, Nonessential, and Conditional

Essential must be consumed in the diet

Nonessential can be synthesized in the body

Conditionally essential cannot be synthesized due to

illness or lack of necessary precursors

Premature infants lack sufficient enzymes needed to create

arginine

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

+ H2O
23

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.
24

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

25

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

26

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.
27

Tertiary Structure

There are four ways in which parts of the amino acid

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

-- 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.
I.

28

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

29

What Are Proteins?

Large molecules

Made up of chains of amino acids

Are found in every cell in the body

Are involved in most of the bodys functions and life processes

The sequence of amino acids is determined by DNA

Structure of Proteins

Made up of chains of amino acids; classified by number of amino acids in a

chain

Peptides: fewer than 50 amino acids

Dipeptides: 2 amino acids

Tripeptides: 3 amino acids

Polypeptides: more than 10 amino acids

Proteins: more than 50 amino acids

Typically 100 to 10,000 amino acids linked together

Chains are synthesizes based on specific bodily DNA

Amino acids are composed of carbon, hydrogen, oxygen, and nitrogen

Characteristics of Proteins
Contain

carbon, hydrogen, oxygen, nitrogen,

and sulfur

Serve

as structural components of animals

Serve

as control molecules (enzymes)

Serve

as transport and messenger

molecules

Basic

building block is the amino acid

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.

33

Denaturing Proteins

Heat

Ultraviolet
Radiation

Strong Acids or
Bases
Urea

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.)

Some Organic
Solvents

Agitation

(e.g. ethanol & acetone) change in dielectric

constant and hydration of ionic groups.
(disinfectant action and precipitation of protein.)
shearing of hydrogen bonds.

34