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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
7
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)
14
Solution AA1
Identify each as (1) polar or (2) nonpolar
CH3
|
CH–OH
|
B. (1) NH2–CH–COOH (Serine)
15
Essential Amino Acids
17
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.
19
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.
20
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
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
26
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”
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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– +
36
Stabilizing protein
37
Learning Check P2
Select the type of tertiary interaction as
(1) disulfide (2) ionic
(3) H bonds (4) hydrophobic
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