Transcript 5 Protein Notes

PROTEINS
June 2, 2016
Functions
1.
2.
Building Blocks
a. Structural components of many cells
Antibodies
a. Involved in defending the body against
foreign invaders
Functions (cont.)
Enzymes
a. Catalyze chemical reactions
b. Examples: Amylase and Lactase
c. They can become Denatured
1. When they lose their function and shape
in extreme conditions
2. Examples: milk souring, cooking eggs
Functions
4.
5.
Signaling
a. Cells signal one another
1. Example: Muscle contraction
Transporters
a. Bind to molecules and carry them to other
cells
Structure
1.
Made up of monomer units called…
 Amino Acids
a. Bonded together through the process of…..

b.
Dehydration Synthesis
Break polymers up through process of…
 Hydrolysis
A
D
B
C
Macromolecule Units Review


Monomer
 Smallest unit of macromolecule
Polymer
 Formed when many monomers bond
How do you make Macromolecules?

Dehydration Synthesis
 Polymers
are formed by removing water from
monomers
How do you break a macromolecule?

Hydrolysis
 Polymers
are broken apart by adding water to break
up into monomers
Functional Groups Commonly Present
1.
Amino Group
2.
Carboxyl Group
Amino Acid Structure
1.
Each Amino Acid has a different combination
of elements labeled simply as its “R Group”
a. 20 total
Amino Acids
Nonpolar
Polar
Acidic
Basic
4 Levels of Structure
1.
Primary Structure
a.
A chain of amino acids
1. Bonds between amino acids
are nonpolar covalent, peptide bonds
Polypeptide Bond
Polypeptide Bond (cont.)
4 Levels of Structure (cont.)
2.
Secondary Structure
a. Arrangement of polypeptide bonds into
different formations
1. Alpha helix: Coil or corkscrew formation
2. Beta Sheet: Pleats or folds
3. Random Coils
b.
Hydrogen bonding present
Hydrogen Bonding: Alpha and Beta
4 Levels of Structure (cont.)
3.
Tertiary Structure
a. 3-D folding of secondary structures
b. Bonding occurring within the protein
1. Hydrophobic interactions occur
2. Ionic Bonds
3. Disulfide bonds
4. Hydrogen bonds
c. At this stage it is a functional protein
Bonding in Tertiary Structure
4 Levels of Structure (cont.)
1.
Quaternary Structure
a.
Tertiary proteins bond with each other, so you have a
group of proteins bonded together
b.
Example: Hemoglobin
Levels of Protein Structure
Level
Primary
Secondary
Tertiary
Quarternary
Types of
bonds
Occur
Between
Ex/Drawings
Description
Level
Types of
bonds
Occur
Between
Primary
Peptide bonds
Amino and
carboxyl groups
on all amino
acids
Secondary
Hydrogen
Bonding
Functional groups Alpha Helix and
(NOT R groups)
Beta Pleated
Sheet
Tertiary
(beginning
of R group
ineractions)
Disulfide
Bonds
Specific polar
aa’s with
exposed sulfur
Cysteinecysteine
Ionic Bonds
Acids and Bases
(+)-(-)
(-) --- (+)
Ionic bond btwn neighboring
acids and bases
Hydrophobic
Interactions
Two nonpolars
CH3-CH3
Hydrophobic R groups want to
get away from anything polar or
charged!
Hydrogen
Bonding
Polar R groups
+ --- -
Any of the
above
Two or more
polypeptides
Quarternary
Ex/Drawings
Description
The NH3 and COOH groups
undergo deyhdration
synthesis
S-S