Chapter 19 Amino Acids and

Proteins
19.1 Proteins and Amino Acids
19.2 Amino Acids as Acids and Bases

Copyright © 2007 by Pearson Education, Inc.

Publishing as Benjamin Cummings

1
Functions of Proteins

Proteins perform many different functions in the body.
TABLE 19.1

2
Amino Acids
Amino acids

Are the building blocks of proteins.

Contain a carboxylic acid group and an amino group
on the alpha (α) carbon.

Are ionized in solution.

Each contain a different side group (R).

R R
│ + │
H2N—C —COOH H3N—C —COO−
│ │
H H
ionized form 3
Examples of Amino Acids
H
+ │
H3N—C—COO−
│
H glycine

CH3
+ │
H3N—C—COO−
│
H alanine 4
 Types of Amino Acids
Amino acids are classified as Nonpolar Polar

Nonpolar (hydrophobic)
with hydrocarbon side
chains.

Polar (hydrophilic) with
polar or ionic side chains. Acidic Basic

Acidic (hydrophilic) with
acidic side chains.

Basic (hydrophilic) with
–NH2 side chains.

5
Copyright © 2007 by Pearson Education, Inc.
Publishing as Benjamin Cummings
 Nonpolar Amino Acids
A nonpolar amino acid has

An R group that is H, an alkyl group, or aromatic.

6
Copyright © 2007 by Pearson Education, Inc.
Publishing as Benjamin Cummings
 Polar Amino Acids
A polar amino acid has

An R group that is an alcohol, thiol, or amide.

Copyright © 2007 by Pearson Education, Inc. 7

Publishing as Benjamin Cummings
 Acidic and Basic Amino Acids
An amino acid is

Acidic with a carboxyl R group (COO−).

Basic with an amino R group (NH3+).
Basic Amino Acids

Copyright © 2007 by Pearson Education, Inc.

8
Publishing as Benjamin Cummings
Learning Check
Identify each as (P) polar or (NP) nonpolar.
+
A. H3N–CH2–COO− (Glycine)

CH3
|
CH–OH
+ │
B. H3N–CH–COO− (Threonine)

9
Solution
Identify each as (P) polar or (NP) nonpolar.
+
A. H3N–CH2–COO− (Glycine) (NP) nonpolar

CH3
|
CH–OH
+ │
B. H3N–CH–COO− (Threonine) (P) polar

10
Fischer Projections of Amino Acids

Amino acids

Are chiral except for glycine.

Have Fischer projections that are stereoisomers.

That are L are used in proteins.

COOH COOH COOH COOH

H2N H H NH2 H2N H H NH2
CH3 CH3 CH2SH CH2SH

L-alanine D-alanine L-cysteine D-cysteine

11
Zwitterions and Isoelectric Points
A zwitterion
• Has charged —NH3+ and COO- groups.
• Forms when both the —NH2 and the —COOH groups
in an amino acid ionize in water.
• Has equal + and − charges at the isoelectric point (pI).

O O
║ + ║
NH2—CH2—C—OH H3N—CH2—C—O–
Glycine Zwitterion of glycine

12
Amino Acids as Acids
In solutions more basic than the pI,

The —NH3+ in the amino acid donates a proton.

+ OH–
H3N—CH2—COO– H2N—CH2—COO–

Zwitterion Negative ion

at pI pH > pI
Charge: 0 Charge: 1−

13
Amino Acids as Bases
In solutions more acidic than the pI,

The COO− in the amino acid accepts a proton.

+ H+ +
H3N—CH2—COO– H3N—CH2—COOH
Zwitterion Positive ion
at pI pH< pI
Charge: 0 Charge: 1+

14
 pH and Ionization

H+ OH−
+ +
H3N–CH2–COOH H3N–CH2–COO– H2N–CH2–COO–
positive ion zwitterion negative ion
(at low pH) (at pI) (at high pH)

15
 Electrophoresis: Separation of
Amino Acids
In electrophoresis, an electric current is used to separate
a mixture of amino acids, and

The positively charged amino acids move toward the
negative electrode.

The negatively charged amino acids move toward the
positive electrode.

An amino acid at its pI does not migrate.

The amino acids are identified as separate bands on
the filter paper or thin-layer plate.

16
 Electrophoresis
With an electric current, a mixture of lysine, aspartate,
and valine are separated.

Copyright © 2007 by Pearson Education, Inc.

Publishing as Benjamin Cummings

17
Learning Check

CH3 CH3
+ | |
H3N—CH—COOH H2N—CH—COO–
(1) (2)
Which structure represents:
A. Alanine at a pH above its pI?
B. Alanine at a pH below its pI?

18
Solution

CH3 CH3
+ | |
H3N—CH—COOH H2N—CH—COO–
(1) (2)
Which structure represents:
A. Alanine at a pH above its pI? (2)
B. Alanine at a pH below its pI? (1)

19
Chapter 19 Amino Acids and
Proteins
19.3
Formation of Peptides

Copyright © 2007 by Pearson Education, Inc

Publishing as Benjamin Cummings
20
The Peptide Bond
A peptide bond

Is an amide bond.

Forms between the carboxyl group of one amino acid and the
amino group of the next amino acid.

O CH3 O
+ || + | ||
H3N—CH2—C—O– + H3N—CH—C—O–

O H CH3 O
+ || | | ||
H3N—CH2—C—N—CH—C—O– + H2O
peptide bond

21
 Formation of A Dipeptide

Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings

22
Learning Check
Write the dipeptide Ser-Thr.
OH CH3
| |
CH2 O HCOH O
+ | ║ + | ║
H3N─CH─C─O – + H3N─CH─C─O–
Ser Thr

23
Solution
Write the dipeptide Ser-Thr.
OH CH3
| |
CH2 O HCOH O
+ | ║ + | ║
H3N─CH─C─O – + H3N─CH─C─O–
Ser peptide Thr
OH bond CH3
| |
CH2 O H HCOH O
+ | ║ | | ║
NH3─CH─C─N ─CH─C─O– + H2O
Ser-Thr
24
 Naming Dipeptides
A dipeptide is named with

A -yl ending for the N-terminal amino acid.

The full amino acid name of the free carboxyl group
(COO-) at the C-terminal end.

Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings

25
Learning Check

Write the three-letter abbreviations and names of the

tripeptides that could form from two glycine and one
alanine.

26
Solution

Write the names and three-letter abbreviations of the

tripeptides that could form from two glycine and one
alanine.
Glycylglycylalanine Gly-Gly-Ala
Glycylalanylglycine Gly-Ala-Gly
Alanylglycylglycine Ala-Gly-Gly

27
Learning Check
What are the possible tripeptides formed from one
each of leucine, glycine, and alanine?

28
Solution
Tripeptides possible from one each of leucine,
glycine, and alanine
Leu-Gly-Ala
Leu-Ala-Gly
Ala-Leu-Gly
Ala-Gly-Leu
Gly-Ala-Leu
Gly-Leu-Ala

29
Learning Check
Write the three-letter abbreviation and name for the
following tetrapeptide:
CH3
│
CH3 S
│ │
CH–CH3 SH CH2
│ │ │
CH3 O H CH2 O H CH2O H CH2 O
+│ ║ │ │ ║ │ │ ║ │ │ ║
H3N–CH–C–N–CH–C–N–CH–C–N–CH–CO–

30
Solution
Ala-Leu-Cys-Met Alanylleucylcysteylmethionine
CH3
│
CH3 S
│ │
CH–CH3 SH CH2
│ │ │
CH3 O H CH O H CH2O H CH2 O
+│ ║ │ │ ║ │ │ ║ │ │ ║
H3N–CH–C–N–CH–C–N–CH–C–N–CH–CO–
Ala Leu Cys Met
31
Chapter 19 Amino Acids and
Proteins
19.4
Protein Structure: Primary and
Secondary Levels

Copyright © 2007 by Pearson Education, Inc

Publishing as Benjamin Cummings

32
Primary Structure of Proteins
The primary structure of a protein is

The particular sequence of amino acids.

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 Copyright © 2007 by Pearson Education, Inc
Publishing as Benjamin Cummings
Ala─Leu─Cys─Met 33
Primary Structures
The nonapeptides oxytocin and vasopressin

Have similar primary structures.

Differ only in the amino acids at positions 3 and 8.

Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings

34
Primary Structure
of Insulin
Insulin

Was the first protein to
have its primary structure
determined.

Has a primary structure of
two polypeptide chains
linked by disulfide bonds.

Has a chain A with 21
amino acids and a chain B
with 30 amino acids.

35
Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings
Secondary Structure – Alpha Helix

The secondary structures of proteins indicate the

three-dimensional spatial arrangements of the
polypeptide chains.

An alpha helix has

A coiled shape held in place by hydrogen bonds
between the amide groups and the carbonyl
groups of the amino acids along the chain.

Hydrogen bonds between the H of a –N-H group
and the O of C=O of the fourth amino acid down
the chain.
36
Secondary Structure – Alpha Helix

Copyright © 2007 by Pearson Education, Inc 37

Publishing as Benjamin Cummings
Secondary Structure – Beta
Pleated Sheet
A beta-pleated sheet is a secondary structure that

Consists of polypeptide chains arranged side by
side.

Has hydrogen bonds between chains.

Has R groups above and below the sheet.

Is typical of fibrous proteins such as silk.

38
Secondary Structure: β-Pleated
Sheet

Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings

39
Secondary Structure: Triple Helix
A triple helix

Consists of three alpha
helix chains woven
together.

Contains large amounts
glycine, proline, hydroxy
proline, and
hydroxylysine that contain
–OH groups for hydrogen
bonding.

Is found in collagen,
connective tissue, skin,
tendons, and cartilage.
40
Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings
Learning Check
Indicate the type of protein structure as
1) primary 2) alpha helix
3) beta-pleated sheet 4) triple helix

A. Polypeptide chains 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.

41
Solution
Indicate the type of protein structure as:
1) primary 2) alpha helix
3) beta-pleated sheet 4) triple helix
A. 3 Polypeptide chains 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.

42
Chapter 19 Amino Acids and
Proteins
19.5
Protein Structure: Tertiary and
Quaternary Levels

Copyright © 2007 by Pearson Education, Inc

Publishing as Benjamin Cummings

43
 Essential Amino Acids
Essential amino acids
TABLE 19.3

Must be obtained
from the diet.

Are the ten amino
acids not
synthesized by the
body.

Are in meat and Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings

diary products.

Are missing (one or
more) in grains and
vegetables.
44
Tertiary Structure

The tertiary structure of a protein

Gives a specific three dimensional shape to the
polypeptide chain.

Involves interactions and cross links between
different parts of the peptide chain.

Is stabilized by
Hydrophobic and hydrophilic interactions.
Salt bridges.
Hydrogen bonds.
Disulfide bonds.

45
Tertiary Structure

The
interactions of
the R groups
give a protein
its specific
three-
dimensional
tertiary
structure.

Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings

46
Tertiary Structure
TABLE 19.5

47
Globular Proteins

Globular proteins Myoglobin

Have compact,
spherical shapes.

Carry out synthesis,
transport, and
metabolism in the
cells.

Such as myoglobin
store and transport
oxygen in muscle.

Copyright © 2007 by Pearson Education, Inc 48

Publishing as Benjamin Cummings
 Fibrous Proteins
Fibrous proteins

Consist of long, fiber-like shapes.

Such as alpha keratins make up hair, wool, skin,
and nails.

Such as feathers contain beta keratins with large
amounts of beta-pleated sheet structures.

Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings 49

Learning Check

Select the type of tertiary interaction

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

50
Solution
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

51
Quaternary Structure
The quaternary structure hemoglobin

Is the combination of two or
more tertiary units.

Is stabilized by the same
interactions found in tertiary
structures.

Of hemoglobin consists of two
alpha chains and two beta
chains. The heme group in
each subunit picks up oxygen
for transport in the blood to the Copyright © 2007 by Pearson Education, Inc
Publishing as Benjamin Cummings

tissues.
52
Summary of Protein Structure

TABLE 19.6

Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings

53
 Summary of Protein Structures

54

Copyright © 2007 by Pearson Education, Inc Publishing as Benjamin Cummings

Learning Check
Identify the level of protein structure as:
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

55
Solution

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.

56
Chapter 19 Amino Acids and
Proteins

19.6
Protein Hydrolysis and Denaturation

Copyright © 2007 by Pearson Education, Inc.

Publishing as Benjamin Cummings
57
Protein Hydrolysis

Protein hydrolysis

Splits the peptide bonds to give smaller peptides
and amino acids.

Occurs in the digestion of proteins.

Occurs in cells when amino acids are needed to
synthesize new proteins and repair tissues.

58
Hydrolysis of a Dipeptide

In the lab, the hydrolysis of a peptide requires acid

or base, water and heat.

In the body, enzymes catalyze the hydrolysis of
proteins.
OH
heat,
CH3 O CH2 O +
+ H2O, H
H3N CH C N CH C OH
H OH
CH3 O CH2 O
+ +
H3N CH COH + H3N CH C OH

59
Denaturation

Denaturation involves

The disruption of bonds in the secondary, tertiary
and quaternary protein structures.

Heat and organic compounds that break apart H
bonds and disrupt hydrophobic interactions.

Acids and bases that break H bonds between polar
R groups and disrupt ionic bonds.

Heavy metal ions that react with S-S bonds to form
solids.

Agitation such as whipping that stretches peptide
chains until bonds break.
60
Applications of Denaturation
Denaturation of protein occurs
when

An egg is cooked.

The skin is wiped with
alcohol.

Heat is used to cauterize
blood vessels.

Instruments are sterilized in
autoclaves.

Copyright © 2007 by Pearson Education, Inc

Publishing as Benjamin Cummings
61
Learning Check

What are the products of the complete hydrolysis of

the peptide Ala-Ser-Val?

62
Solution

The products of the complete hydrolysis of the

peptide Ala-Ser-Val are

alanine
serine
valine

63
Learning Check

Tannic acid is used to form a scab on a burn. An

egg is hard boiled by placing it in boiling water.
What is similar about these two events?

64
Solution
Acid and heat cause the denaturation of protein.
They both break bonds in the secondary and tertiary
structures of proteins.

65