Amines

• Organic compounds of nitrogen N

• Classified as primary, secondary, tertiary
CH3 CH3
 
CH3—NH2 CH3—NH CH3—N — CH3

1° 2° 3°

1
 Naming Amines
IUPAC aminoalkane Common alkylamine
CH3CH2NH2 CH3—NH —CH3
aminoethane N-methylaminomethane
(ethylamine) (dimethylamine)
NH2
NH CH3
NH2
|
CH3CHCH3
2-aminopropane Aniline N-methylaniline
(isopropylamine)

2
 Amides
Derivatives of carboxylic acids where an
amino (-NH2) group replaces the –OH
group.
O O
 
CH3 — C—OH CH3 — C—NH2
carboxylic acid amide
acetic acid acetamide
3
 Naming Amides
Alkanamide from acid name
O
 methanamide (IUPAC)
HC–NH2 formamide (common)

O
 propanamide (IUPAC)
CH3CH2C–NH2 propionamide(common)
4
 Naming Amides with N-Groups
O

CH3C–NHCH3 N-methylethanamide (IUPAC)
N-methylacetamide (common)
O

CH3CH2C–N(CH3)2
N,N-dimethylpropanamide
N,N-dimethylpropionamide
5
Amino Acids Proteins, and
Enzymes
Types of Proteins
Amino Acids
The Peptide Bond

6
 Types of Proteins
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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 Amino Acids
• Building blocks of proteins
• Carboxylic acid group
• Amino group
• Side group R gives unique characteristics

R side chain
I
H2N—C —COOH
I
H 8
 Examples of Amino Acids
H
I
H2N—C —COOH
I
H glycine
CH3
I
H2N—C —COOH
I
H alanine 9
 Types of Amino Acids
Nonpolar R = H, CH3, alkyl groups, aromatic
O
Polar ll
R = –CH2OH, –CH2SH, –CH2C–NH2,
(polar groups with –O-, -SH, -N-)
Polar/Acidic
R = –CH2COOH, or -COOH
Polar/ Basic
R = –CH2CH2NH2 10
Nonpolar R groups

11
Polar R groups.

12
Polar R groups

13
 Learning Check AA1
Identify each as (1) polar or (2) nonpolar

A. NH2–CH2–COOH (Glycine)

CH3
|
CH–OH
|
B. NH2–CH–COOH (Serine)
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 Solution AA1
Identify each as (1) polar or (2) nonpolar

A.(2) NH2–CH2–COOH (Glycine)

CH3
|
CH–OH
|
B. (1) NH2–CH–COOH (Serine)
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 Essential Amino Acids

• 10 amino acids not synthesized by the

body
• arg, his, ile, leu, lys, met, phe, thr, trp, val
• Must obtain from the diet
• All in diary products
• 1 or more missing in grains
and vegetables
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Amino Acids as Acids and Bases

• Ionization of the –NH2 and the –COOH group

• Zwitterion has both a + and – charge
• Zwitterion is neutral overall
+
NH2–CH2–COOH H3N–CH2–COO–
glycine Zwitterion of glycine

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 pH and ionization

H+ OH–
+ +
H3N–CH2–COOH H3N–CH2–COO– H2N–CH2–COO–
Positive ion zwitterion Negative ion
Low pH neutral pH High pH

18
 Learning Check AA2
CH3 CH3
+
H3N–CH–COOH H2N–CH2–COO–
(1) (2)
Select from the above structures
A. Alanine in base.
B. Alanine in acid.
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 Solution AA2
CH3 CH3
+
H3N–CH–COOH H2N–CH2–COO–
(1) (2)
Select from the above structures
A. (2) Alanine in base.
B. (1) Alanine in acid.
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 The Peptide Bond
Amide bond formed by the –COOH of an amino
acid and the –NH2 of the next amino acid
O CH3
+ || + |
NH3–CH2–CO – + H3N–CH–COO–
O CH3
+ || |
NH3–CH2–C – N–CH–COO–
| peptide bond
H

21
 Naming Amides with N-Groups
O

CH3C–NHCH3 N-methylethanamide (IUPAC)
N-methylacetamide (common)
O

CH3CH2C–N(CH3)2
N,N-dimethylpropanamide
N,N-dimethylpropionamide
22
 Peptides
• Amino acids linked by amide (peptide) bonds

Gly Lys Phe Arg Ser

H2N- -COOH
end Peptide bonds end

Glycyllysylphenylalanylarginylserine
23
 Learning Check AA3
What are the possible tripeptides formed
from one each of leucine, glycine, and
alanine?

24
 Solution AA3
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
25
 Learning Check AA4
Write the three-letter abbreviations for the
following tetrapeptide:

CH3
CH3 S
CH CH3 SH CH2
CH3 O CH O CH 2 O CH2 O
-
H3N CH C N CH C N CH C N CH C O
H H H
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27
 Solution AA4
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

28
 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 29
 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”

30
31
 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

32
Pleated sheet

33
 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

34
Collagen
and
pleated
sheet

35
 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–

36
Stabilizing protein

37
 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
38
Leucine and Valine

39
Two Cysteines

40
Aspartic Acid and Lysine

41
Serine and Threonine

42
 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

43
Permanent
wave

44