Amino Acids, Proteins, and

Enzymes
Primary and Secondary Structure
Tertiary and Quaternary Structure
Protein Hydrolysis and Denaturation

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 Primary Structure of Proteins
The particular sequence of amino acids
that is the backbone of a peptide chain or
protein CH3
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 2
 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

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 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
(2) primary (2) alpha helix
(3) beta pleated sheet (4) triple helix

E. Polypeptide chain held side by side by H bonds

F. Sequence of amino acids in a polypeptide chain
G. Corkscrew shape with H bonds between amino
acids
H. Three peptide chains woven like a rope

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 Solution P1
Indicate the type of structure as
(2) primary (2) alpha helix
(3) beta pleated sheet (4) triple helix

• 3 Polypeptide chain held side by side by H bonds

• 1 Sequence of amino acids in a polypeptide chain
• 2 Corkscrew shape with H bonds between amino
acids
• 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
H. 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
• 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

F. Beta pleated sheet

G. Order of amino acids in a protein
H. A protein with two or more peptide chains
I. The shape of a globular protein
J. 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

• 2 Beta pleated sheet

• 1 Order of amino acids in a protein
• 4 A protein with two or more peptide
chains
D. 3 The shape of a globular protein
E. 3 Disulfide bonds between R groups 14
 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
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 Hydrolysis of a Dipeptide

OH

+
CH3 O CH 2 O H2O, H +
H3N CH C N CH C OH
H heat
OH
CH3 O CH 2 O
+ +
H 3N CH COH + H 3N CH C OH

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 Denaturation
Disruption of secondary, tertiary and quaternary protein
structure by
heat/organics
Break apart H bonds and disrupt hydrophobic
attractions
acids/ bases
Break H bonds between polar R groups and
ionic bonds
heavy metal ions
React with S-S bonds to form solids
agitation
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Stretches chains until bonds break
 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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