Beruflich Dokumente
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Goals/Key questions
Goals: Students will learn about biochem units
Objective: catch up with schedule, explain the role of cellular respiration in detail
GLEs/SLEs addressed:
20D1.2k describe the chemical nature of carbohydrates, lipids and proteins and their enzymes; i.e., carbohydrases, lipases and
proteases
20D1.3k explain enzyme action and factors influencing their action; i.e., temperature, pH, substrate concentration, feedback
inhibition, competitive inhibition
Lab tomorrow
Monomer
a molecule that can be bonded to other identical
molecules to form a polymer
Polymer
consisting of two monomers
1
Proteins
Purposes
1) Cell Structure
Major part of muscle, skin, nerves
Required for the building, repair and maintenance of cell structure.
Proteins
Purposes
2) Cell Function
Chemical messenger -- hormones
Transport -- hemoglobin
Movement -- contractile proteins
Catalysis of cell reactions -- enzymes
Defense against foreign substances -- antibodies
Proteins
Structure
Contains CHON
Carbon, Hydrogen, Oxygen, NITROGEN
Proteins
Terms
Protein
A large molecule made of one or more polypeptide chains folded and Think pair share
coiled into a specific shape.
Polypeptide Chains
polymers of amino acids arranged in a specific order and linked by
peptide bonds
Peptide Bond
Covalent bond between adjacent amino acids
Proteins
Amino Acids
The structural subunit of proteins
20 Different types
8 are essential
Cannot be manufactured by the body
Must be obtained from food
Structure...
Amino Acid Structure
Peptide bond formation
Polypeptide Chain 1 Protein
Levels of Protein Structure
Primary Structure
determined by the genes on the chromosomes
Levels of Protein Structure
Primary Structure
different protein has a different sequence and number of amino acids
Levels of Protein Structure
Primary Structure
The primary structure - the linear sequence of amino acids in the
polypeptide chain.
Levels of Protein Structure
Primary Structure
Held together by covalent bonds such as peptide bonds
Amino acids are organized in a linear arrangements
2
Primary Protein
Primary Structure
Types of Proteins
Secondary Structure
The amino acid chains are coiled or folded due to hydrogen bonding.
Secondary Protein
Secondary Structure
Types of Proteins
Primary
organized into linear arrangements
Secondary
The amino acid chains are coils
Hydrogen bonds cause this.
Tertiary
The coiled molecule is further twisted into a folded 3-D shape
Tertiary Protein
Types of Proteins
Primary
organized into linear arrangements
Secondary
The amino acid chains are coils
Hydrogen bonds cause this.
Tertiary
The coiled molecule is further twisted into a folded 3-D shape
Quaternary
globular proteins formed from the interaction between different protein
chains
Example: hemoglobin, enzymes
Tertiary and Quaternary Structure
Draw the different types of proteins
Quaternary Protein
Protein Changes
Denaturation
Coagulation
Protein Changes
Denaturation
Changes in the shape of the protein by physical or chemical factors such
as heat, radiation or pH changes.
Protein may uncoil or assume a new shape.
Proteins physical properties and biological properties are changed.
Protein Changes
Coagulation
Permanent change in the shape of the protein
e.g. boiling egg white
https://www.youtube.com/watch?time_continue=92&v=gEycDKQn93Y
exit slip 1
-solution 1
3
Transition considerations Noise space
Sitting time
Conclusion Homework
Time Est: 3 minutes Pg 216 1,3,5,7
Assessment: exit slip