Proteins

• Functions
• Primary, Secondary, Tertiary and Quaternary
Structure
• Protein Hydrolysis
and Denaturation

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PROTEINS
• From the Greek
“proteios,” meaning
first,
are a class of organic
compounds which are
present in and vital to
every living cell

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 Proteins
Do Most of the Work
of the Cell

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Proteins Do Most of the Work of the Cell …

1. Every cell has

thousands of
different types of
proteins, each
specialized to do a
certain job.

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Proteins Do Most of the Work of the Cell …

2. Some proteins are

structural: control
shape of cells and
bind cells together
Example: collagen-
binds all of the cells
of the body together

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Proteins Do Most of the Work of the Cell …

3. Chemical
reactions of the
cell are
controlled by
PROTEIN
ENZYMES

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Proteins Do Most of the Work of the Cell …

4. PROTEIN
PUMPS
move things
across the
cell
membrane
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Proteins Do Most of the Work of the Cell …

5. Proteins give
mobility:
Muscles
    Flagella
    "Molecular
motors"

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Proteins Do Most of the Work of the Cell …

6. Defend the
body against
foreign
invaders:
antibodies.

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Proteins Do Most of the Work of the Cell …

7. Receptors:
required for
signalling in
endocrine and
nervous
systems.
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 Proteins are Made up of Exactly
20 Types of Amino Acids
the proteins in our bodies are made of 20
different amino acids strung together like beads
on a string.
All 20 have a part in common: a central carbon
attached to a carboxyl, an amino and a hydrogen
atom.
The differences between the 20 types are in the
side groups that can be designated as R.
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 Proteins are Amino Acids Linked
Together by Peptide Bonds
• In proteins the carboxyl group (COOH) of one
amino acid attaches to the amine group (NH2)
of the next to form a peptide bond.
• The reaction requires ATP
• Water is removed
• Protein chains are not branched
Note that the R groups stick out to the side of the
protein chain
Each protein has a terminal amino group on one
end and a terminal carboxyl on the other end
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– The Side Groups of
Proteins can be hydrophobic
or Hydrophilic
The 20 different R groups fall naturally into 2
classes, those that like water (hydrophilic) and
those that hate water (hydrophobic).
Hydrophobic side groups are nonpolar (no partial
charges): attracted to lipids or to other
hydrophobic groups
Hydrophilic side groups are polar: side group has
a partial + charge at one end and a partial -
charge at the other: attracted to water

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• The SHAPES OF PROTEINS are
Determined by Hydrogen
Bonding and by the Numbers and
Sequence of the Side Groups

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   Some hydrophilic side groups are charged:
these are sensitive to pH
  Carboxyls (COOH) can lose H ion, become
negatively charged
 Amines (NH2) can take up a H ion,
become positively charged, the hydrophobic
amino acids are likely to be imbedded in
other hydrophobic structures, such as the
interiors of membranes or the hydrophobic
side groups of another part of the same
protein.
  To cross a membrane a protein must have a
stretch of 20 to 25 amino acids which are
mostly hydrophobic.
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 Types of Proteins
(according to functions)
Type Examples
• Structural tendons, cartilage, hair, nails
• Contractile muscles
• Transport hemoglobin
• Storage milk
• Hormonal insulin, growth hormone
• Enzyme catalyzes reactions in cells
• Protection immune response

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 Primary Structure of Proteins

---The particular sequence of amino

acids that is the backbone of a
peptide chain or protein CH 3
CH3 S
CH CH3 SH CH2
CH3 O
+ CH O CH2 O CH2 O
-
H3N CH C N CH C N CH C N CH C O
H H H

Ala-Leu-Cys-Met 17
• Primary structure of a protein is
the sequence of amino acids.
Each protein has a unique
sequence determined by the
genetic code (no substitutions
allowed)
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Secondary Structure –
Alpha Helix

• Three-dimensional arrangement of
amino acids with the polypeptide chain
in a corkscrew shape
• Held by H bonds between the H of –N-
H group and the –O of C=O of the
fourth amino acid along the chain
• Looks like a coiled “telephone cord”
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 Secondary Structure –
Beta Pleated Sheet
• Polypeptide chains are
arranged side by side
• Hydrogen bonds form
between chains
• R groups of extend above and
below the sheet
• Typical of fibrous proteins
such as silk 20
 Secondary Structure –
Triple Helix
• Three polypeptide chains woven
together
• Glycine, proline, hydroxy proline
and hydroxylysine
• H bonding between –OH groups
gives a strong structure
• Typical of collagen, connective
tissue, skin, tendons, and
cartilage
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 Learning Check P1
Indicate the type of structure as
(1) primary (2) alpha helix
(3) beta pleated sheet (4) triple helix
A. Polypeptide chain held side by side by H
bonds
B. Sequence of amino acids in a polypeptide
chain
C. Corkscrew shape with H bonds between
amino acids
D. Three peptide chains woven like a rope
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 Solution P1
Indicate the type of structure as
(1) primary (2) alpha helix
(3) beta pleated sheet (4) triple helix

A. 3 Polypeptide chain held side by side by H

bonds
B. 1 Sequence of amino acids in a polypeptide
chain
C. 2 Corkscrew shape with H bonds between
amino acids
D. 4 Three peptide chains woven like a rope
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 Tertiary Structure
• Specific overall shape of a protein
• Cross links between R groups of
amino acids in chain
disulfide –S–S– +

ionic –COO– H3N–

H bonds C=O HO–
hydrophobic –CH3, H3C–

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 Learning Check P2

Select the type of tertiary interaction as

(1) disulfide (2) ionic
(3) H bonds (4) hydrophobic

A. Leucine and valine

B. Two cysteines
C. Aspartic acid and lysine
D. Serine and threonine
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 Solution P2

Select the type of tertiary interaction as

(1) disulfide (2) ionic
(3) H bonds (4) hydrophobic
A. 4 Leucine and valine
B. 1 Two cysteines
C. 2 Aspartic acid and lysine
D. 3 Serine and threonine
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 Globular and Fibrous Proteins

Globular proteins Fibrous proteins

“spherical” shape long, thin fibers
Insulin Hair
Hemoglobin Wool
Enzymes Skin
Antibodies Nails

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 Quaternary Structure
• Proteins with two or more chains
• Example is hemoglobin
• Carries oxygen in blood
Four polypeptide chains
Each chain has a heme group
to bind oxygen
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 Learning Check P3
Identify the level of protein structure
1. Primary 2. Secondary
3. Tertiary 4. Quaternary

A. Beta pleated sheet

B. Order of amino acids in a protein
C. A protein with two or more peptide chains
D. The shape of a globular protein
E. Disulfide bonds between R groups

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 Solution P3

Identify the level of protein structure

1. Primary 2. Secondary
3. Tertiary 4. Quaternary

A. 2 Beta pleated sheet

B. 1 Order of amino acids in a protein
C. 4 A protein with two or more peptide
chains
D. 3 The shape of a globular protein
E. 3 Disulfide bonds between R groups
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Protein Properties
are Determined by
their Shapes

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  A typical protein will have 200
to 1000 amino acids. A molecule
this big can bend into millions of
different shapes, but only one is
correct
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 Proteins will not function
        

unless folded into proper

shape. Like any machine,
the parts must be in the right
positions before it can work 33
Protein shape is disrupted
by many agents, especially
heat- this is called
denaturation

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Many proteins have"active
sites" produced by side
groups brought together by
folding

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Heat sterilizes by
denaturing
proteins of
bacteria and
viruses
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 Protein Hydrolysis
• Break down of peptide bonds
• Requires acid or base, water
and heat
• Gives smaller peptides and
amino acids
• Similar to digestion of
proteins using enzymes
• Occurs in cells to provide
amino acids to synthesize
other proteins and tissues 37
 Hydrolysis of a Dipeptide
OH
CH3 O CH2 O +
+ H2O, H
H3N CH C N CH C OH
H heat
OH
CH3 O CH2 O
+ +
H3N CH COH + H3N CH C OH
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 Denaturation
Disruption of secondary, tertiary and quaternary
protein structure by
1. heat/organics
Break apart H bonds and disrupt hydrophobic
attractions
2. acids/ bases
Break H bonds between polar R groups and
ionic bonds
3. heavy metal ions
React with S-S bonds to form solids
4. agitation
Stretches chains until bonds break 39
Applications of Denaturation
• Hard boiling an egg
• Wiping the skin with alcohol swab
for injection
• Cooking food to destroy E. coli.
• Heat used to cauterize blood
vessels
• Autoclave sterilizes instruments
• Milk is heated to make yogurt
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 Learning Check P4

What are the products

of the complete
hydrolysis of
Ala-Ser-Val ?
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 Solution P4

The products of the complete

hydrolysis of Ala-Ser-Val are

alanine
serine
valine
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 Learning Check P5

Tannic acid is used to form a

scab on a burn. An egg becomes
hard boiled when placed in hot
water. What is similar about
these two events?

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 Solution P5

Acid and heat cause a

denaturation of protein.
They both break bonds in
the secondary and tertiary
structure of protein.
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end
of the
lecture !
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