19.1 Proteins and Amino Acids

Chapter 19 Amino Acids and
Proteins
19.1
Proteins and Amino Acids
• Classify proteins by their functions in the body. Give the name

and abbreviation of an amino acid and draw its ionized structure.
General, Organic, and Biological Chemistry Copyright © 2010 Pearson Education, Inc. 1
Functions of Proteins
Function of protein p - 673
 Proteins perform many different functions in the body.
Amino Acids
Amino acids
 are the building blocks of proteins
 contain a carboxylic acid group and an amino group
on the alpha () carbon
 are ionized in solution
 each contain a different side group (R)
Examples of Amino Acids
Types of Amino Acids
Amino acids are classified as Nonpolar Polar (neutral)
 nonpolar with hydrocarbon
side chains (hydrophobic)
 polar (neutral) with polar
or ionic side chains
(hydrophilic) Acidic Basic
 polar (acidic) with acidic
side chains (hydrophilic)
 polar (basic) with
–NH2 side chains
(hydrophilic)
Nonpolar Amino Acids
A nonpolar amino acid has an R group that is H, an
alkyl group, or aromatic.
Polar (Neutral) Amino Acids
A polar amino acid has an R group that is an alcohol,
thiol, or amide.
Polar (Acidic) and Polar (Basic)
Amino Acids
An amino acid is
 acidic with a carboxyl R group (COO–)
 basic with an amino R group (NH3+)
Learning Check
Identify each of the following as a polar (P) or nonpolar
(NP) amino acid.
Solution
Identify each of the following as a polar (P) or nonpolar
(NP) amino acid.
Nonpolar (NP)
Polar (P)
Proteins
19.2
Amino Acids as Zwitterions
Draw the zwitterion of an amino acid at its isoelectric point and its
ionized structure at pH values above or below its isoelectric point.
Zwitterions and Isoelectric Points
A zwitterion
 has an equal number of —NH3+ and COO– groups
 forms when the H from —COOH in an amino acid
transfers to the —NH2
Isoelectric Point (pI)
The isoelectric points (pI)
 are the pH at which zwitterions have an overall zero
charge
 of nonpolar and polar (neutral) amino acids exist at pH
values from 5.1 to 6.3
Zwitterions in Acidic Solutions
In solutions that are more acidic than the pI,
 the COO– in the zwitterion accepts a proton
 the amino acid has a positive charge
Glycine, with a pI of 6.0, has a 1+ charge in solutions

that have a pH below pH 6.0.
Zwitterions in Basic Solutions
In solutions that are more basic than the pI,
 the NH3+ in the zwitterion loses a proton
 the amino acid has a negative charge
Glycine, with a pI of 6.0, has a 1– charge in solutions

that have a pH above pH 6.0.
pI, pH, and Charge
Summary of pH, pI, and
Ionization
Ionized Forms of Polar (Acidic)
and Polar (Basic) Amino Acids
Polar (acidic) and polar (basic) amino acids
 also ionize the —COO and —NH3+ in their polar R
groups
 Zwitterions of polar (acidic) amino acids exist at pH
values from 2.8 to 3.2.
 Zwitterions of polar (basic) amino acids exist at pH
values from 7.6 to 10.8.
Zwitterions of Aspartic Acid
Aspartic acid, a polar (acidic) amino acid,
 has a pI of 2.8
 forms a zwitterion at pH 2.8
 forms negative ions with charges 1– and 2– at pH
values greater than pH 2.8
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
Electrophoresis
With an electric current, a mixture of lysine, aspartate,
and valine are separated.
Electrophoresis
Used to screen for sickle cell trait in newborns
Learning Check
Which structure represents:

A. alanine at a pH above its pI?
B. alanine at a pH below its pI?
Solution
Which structure represents:

A. alanine at a pH above its pI? (2)
B. alanine at a pH below its pI? (1)
Proteins
19.3
Formation of Peptides
• Draw the structure of a dipeptide.

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
 contains an N (free H3N+) terminal written on the left
 contains a C (free COO –) terminal written on the right
Formation of a Dipeptide
Naming Dipeptides Structure of protein p - 680
A dipeptide is named with

 a yl ending for the N-terminal (free H3N+) amino acid
 the full amino acid name of the free carboxyl group
(COO–) at the C-terminal end
Learning Check
Draw the condensed structural formula, and give the
name and abbreviation for the dipeptide Ser-Thr.
Solution
Proteins
19.4
Protein Structure: Primary
and Secondary Levels
• Describe the primary and secondary structures of a protein.

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
Ala─Leu─Cys─Met
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 an A chain with 21
amino acids and a B chain
with 30 amino acids
H.N. P 684
Polypeptide in the body

The nonapeptides oxytocin and vasopressin
 have similar primary structures
 differ only in the amino acids at positions 3 and 8
Secondary Structure: Alpha Helix
The secondary structures of proteins indicate the
three-dimensional spatial arrangements of the
polypeptide chains.
An alpha helix (α-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 an —NH group
and the O of C═O of the fourth amino acid down
the chain
Secondary Structure: Alpha Helix
(continued)
Secondary Structure: Beta-Pleated
Sheet
A beta-pleated sheet (β-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
Secondary Structure: Beta-Pleated
Sheet (continued)
Secondary Structure: Triple Helix
A triple helix
 consists of three alpha helix
chains woven together
 contains large amounts of
glycine, proline, hydroxyproline,
and hydroxylysine that contain
–OH groups for hydrogen
bonding
 is found in collagen, connective
tissue, skin, tendons, and
cartilage
Primary & secondary Structure
p 684
H.N. P 687
Essential Amino Acids
Essential amino acids
 are the ten amino
acids not synthesized
by the body
 must be obtained from
the diet
 are in meat and diary
products
 are missing (one or
more) in grains and
vegetables
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
Solution
Indicate the type of protein structure as:
1) primary 2) alpha helix
3) beta-pleated sheet 4) triple helix
3 A. polypeptide chains held side by side by H

bonds
1 B. sequence of amino acids in a polypeptide
chain
2 C. corkscrew shape with H bonds between amino
acids
4 D. three peptide chains woven like a rope
Proteins
19.5
Protein Structure: Tertiary
and Quaternary Levels
• Describe the tertiary and quaternary structures of a protein.

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
Tertiary Structure (continued)
 The interactions of
the R groups give
a protein its
specific three-
dimensional
tertiary structure.
Cross-Links in Tertiary Structures
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
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
Learning Check
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
Solution
Select the type of tertiary interaction as:
1) disulfide 2) ionic
3) H bonds 4) hydrophobic
4 A. leucine and valine

1 B. two cysteines
2 C. aspartic acid and lysine
3 D. serine and threonine
Quaternary Structure
Tertiary & Quaternary
Structure of proteins p 687
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 with heme
groups in each subunit that
pick up oxygen for transport
in the blood to the tissues
Hemoglobin & Myoglobin
 Have similar biological functions.
 Hemoglobin carry oxygen in blood while Myoglobin

carry oxygen in muscle.
 Myoglobin, a single polypeptide is identical to tertiary

structure of each subunit of hemoglobin (4 units)
 Myoglobin stores one oxygen whereas hemoglobin

stores 4 oxygen.
Summary of Protein Structures
(continued)
Summary of Protein Structures
Sickle – Cell Anemia H.N. P 692
 Caused by abnormality in the

shape of one of the
hemoglobin subunits. (β-chain)
 The shape of RBC changed.
 Less oxygen is transported.
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
Solution
Identify the level of protein structure as:
1) primary 2) secondary
3) tertiary 4) quaternary
2 A. beta-pleated sheet
1 B. order of amino acids in a protein
4 C. a protein with two or more peptide chains
3 D. the shape of a globular protein
3 E. disulfide bonds between R groups
Proteins
19.6
Protein Hydrolysis and Denaturation
• Describe the hydrolysis and denaturation of proteins.

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
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.
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
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
an autoclave
Learning Check
What are the products of the complete hydrolysis of
the tripeptide Ala-Ser-Val?
Solution
What are the products of the complete hydrolysis of
the tripeptide Ala-Ser-Val?
The products are the three amino acids: alanine,

serine, and valine.
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?
Solution
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?
Acid and heat cause the denaturation of protein. They

both break bonds in the secondary and tertiary
structures of proteins.

19.1 Proteins and Amino Acids

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19.1 Proteins and Amino Acids

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Chapter 19 Amino Acids and

• Classify proteins by their functions in the body. Give the name

 Proteins perform many different functions in the body.

Glycine, with a pI of 6.0, has a 1+ charge in solutions

Glycine, with a pI of 6.0, has a 1– charge in solutions

Which structure represents:

Which structure represents:

• Draw the structure of a dipeptide.

A dipeptide is named with

• Describe the primary and secondary structures of a protein.

Polypeptide in the body

An alpha helix (α-helix) has

A. polypeptide chains held side by side by H bonds

3 A. polypeptide chains held side by side by H

• Describe the tertiary and quaternary structures of a protein.

A. leucine and valine

4 A. leucine and valine

The quaternary structure Hemoglobin

 Have similar biological functions.

 Hemoglobin carry oxygen in blood while Myoglobin

 Myoglobin, a single polypeptide is identical to tertiary

 Myoglobin stores one oxygen whereas hemoglobin

 Caused by abnormality in the

 The shape of RBC changed.

 Less oxygen is transported.

• Describe the hydrolysis and denaturation of proteins.

The products are the three amino acids: alanine,

Acid and heat cause the denaturation of protein. They

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