2. Monomer
The single unit that makes up a protein is an
amino acid
Question: Based on its name, which 2
functional groups would be found in an amino
acid?
An amino acid is sometimes referred to as a
residue
3. Amino acid structure
four components attached to a central carbon:
amino group H
carboxylic acid (carboxyl) group |
hydrogen atom H2N – C – COOH
|
variable R group (or side chain) R
Question: Determine which functional group is
acidic and basic. Explain how you know.
4. Amino acid structure
H
Amphiprotic: containing both |
acidic and basic functional groups H2N – C – COOH
|
The ionized form is observed in R
aqueous solutions because the +H2O
acidic group can donate H+ ion to H
the basic group |
+H N
3 – C – COO-
|
R
5. Amino acid R groups (side chains)
differences in R groups produce the 20
different amino acids
8 are essential: body cannot synthesize them
6. Amino acid R groups (side chains)
Physical and chemical characteristics of the R
group determine the unique characteristics of
an amino acid
Amino acids are classified into 4 groups
based on their R groups:
Nonpolar H
|
Polar
H2N – C – COOH
Acidic |
basic R
7. Activity
Given the 20 amino acids, group them into
the 4 categories based on the properties of
their R groups
The 4 categories are:
Nonpolar
Polar
Acidic
basic
13. Protein shape determines function
Amino acid order determines the shape
(conformation) of a protein
Conformation determines function
Function depends on its ability to recognize
and bind a molecule
Amino acids conformation function binding
14. Protein binding examples
Antibodies bind to particular foreign
substances that fit their binding sites.
Enzymes recognize and bind to specific
substrates, facilitating a chemical reaction.
Neurotransmitters pass signals from one cell
to another by binding to receptor sites on
proteins in the receiving cell.
15. Levels of protein structure
Primary (1o)
organizes folding within
Secondary (2o)
a single polypeptide
Tertiary (3o)
interactions between two
Quaternary (4o) or more polypeptides that
make a protein
22. Tertiary (3o) Structure: Proline kink
Proline is the only amino acid in which the R
group is attached to the amino group
Forms a natural kink in the polypeptide
Helps to shape tertiary structure
25. Quaternary (4o) Structure: Fibrous
Water insoluble
Threadlike
Example: collagen
3 polypeptides supercoiled
like a rope
provides structural strength
for role in connective tissue
28. Tutorial: Protein Folding
http://www.wiley.com/legacy/college/boyer/0470003790/ani
mations/protein_folding/protein_folding.htm
29. Conformational Change
Changing the shape of a protein
Reversible
Does not disrupt a proteins function but
rather is what defines the protein’s function
Change occurs in response to the physical
and chemical conditions.
32. Denaturation
Renaturation: some proteins can return to
their functional shape after denaturation
But others cannot, especially in the crowded
environment of the cell.
34. HW Question
Contrast secondary and tertiary levels of
protein structure. [2 marks]
Compare conformational change and
denaturation. Use an example. [3 mark]