Proteins
SBI4U
Amino Acids
H
H
C
O
Amino Acids
Alpha () Carbon
H
Amino Group
H
R
These 3 groups are common
to ALL amino acids
O
C
O
Carboxyl Group
Amino Acids
H
H
O
C
O
Amino Acids
Classified into 4 different groups:
Hydrophobic/
Non-Polar
Methionine
Proline
Alanine
Valine
Leucine
Isoleucine
Tryptophan
Phenylalanine
Amino Acids
Classified into 4 different groups:
Polar/Hydrophilic
Uncharged
Tyrosine
Glycine
Serine
Threonine
Cysteine
Glutamine
Asparagine
Amino Acids
Classified into 4 different groups:
Polar/Hydrophilic
Acidic/Negative
Glutamic Acid
Aspartic Acid
Amino Acids
Classified into 4 different groups:
Polar/Hydrophilic
Basic/Positive
Lysine
Arginine
Histidine
Discuss the
properties of your
amino acid with
your group
Bond Formation
H
H
H
H
CH3
Dehydration Synthesis
N
O
O
C
O
Bond Formation
H
H
H
CH3
N
O
O
C
O
Bond Formation
H
Peptide Bond
H
CH3
N
O
Dipeptide
O
C
O
Peptides
Dipeptide: Two amino acids
Oligopeptide: less than 10 amino acids
Polypeptide: 10 or more amino acids
Create a dipeptide
with your partner
Create an
oligopeptide with
your group
Structure
Primary Structure: Sequence of
amino acids
Secondary structure: alpha helices
and beta sheets
Tertiary structure: R group
interactions
Quaternary structure: Polypeptides
associating together
Primary Structure
Order the amino acids are
bonded
Secondary Structure
Hydrogen bonding between
the backbone of the peptide
Alpha helices
Beta pleated sheets
Tertiary Structures
The 3D shape of the protein
Proteins can be functional at
this point
Function depends on
structure
Formed based on
interactions with R groups
After this stage it can be
called a protein
The protein is in its native
state
Quaternary Structure
Multiple protein units
associated together
DEnaturation
Process where proteins lose their
structure while maintaining their
primary structure
Can be reversible
Extreme cases are irreversible
Caused by stress on protein:
1. Heat
2. Strong acid or base
3. Concentrated salt