Biology for Life

  Skyline High School IB Biology

 
 

  Units of Study

Science of Biology
Prokaryotic Cells
Eukaryotic Cells
Basics of Biochemistry
DNA and Electrophoresis
Cell Cycle & DNA Replication
Protein Synthesis & Mutations
Protein Structure & Function
Genetic Technology
Viruses
Classification & Phylogenies
Diversity of Life
Theoretical Genetics
Meiosis and Reproduction
Variation and Evolution
Origins and Speciation
Human Evolution
Ecosystems & Energy Flow
Circulatory system
Respiratory system
Cellular Respiration
Photosynthesis
Digestion
The Kidney 
The Liver
Skeletal System
Immune System
Endocrine System
The Nervous System
Nutrient Cycles
Human Effects
Communities & Succession
Earth's Biomes
Diversity and Conservation
Population Dynamics
Population Genetics
Plant structure and Growth
Plant Transport
Angiosperm Reproduction
Enzyme Action
Muscles and Movement
Behavior

 

 

 

 

 

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Assessment Statements:

 

7.5.2

Outline the difference between fibrous and globular proteins, with reference to two examples of each protein type.

 

7.5.4

State four functions of proteins, giving a named example of each.

7.4.5

Draw and label a diagram showing the structure of a peptide bond between two amino acids.

 

3.2.2

Identify amino acids ... from diagrams showing their structure.

 

3.2.5

Outline the role of condensation and hydrolysis in the relationships between … amino acids and polypeptides

 

7.5.1

Explain the four levels of protein structure, indicating the significance of each level.

 

7.5.3

Explain the significance of polar and non-polar amino acids.

 

3.6.4

Define denaturation.

 

 

 

 

 

 

 

 

 

 

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What You Should Be Able to Do

 

Protein Structure

  • Draw the generalized amino acid structure, identifying the amino group, the carboxyl group, the radical group, and the alpha carbon.

  • Define what is meant by “essential amino acid.”

  • Explain how the characteristics of R groups (polar, non-polar, and ionic) affect their behavior in protein folding.

  • Describe polypeptide chain formation in terms of the formation of peptide bonds and condensation reactions.

  • Determine the number of peptide bonds given the number of amino acids in a polypeptide.

  • Describe the primary structure of a protein, including the type of bonding involved.

  • Describe the secondary structure of a protein, including the type of bonding involved.

  • Describe the tertiary structure of a protein, including the types of bonding involved.

  • Describe the quaternary structure of a protein.

  • Explain the role of chaperones in protein folding.

  • Contrast the structure of globular proteins with the structure of fibrous proteins.

  • Define denaturation and list conditions that can cause it to happen.

Protein Function

  • Define proteomics.

  • Contrast the generalized function of globular proteins with generalized function of fibrous proteins.

  • List and describe examples of fibrous proteins used in structure and support.

  • List and describe examples of fibrous proteins used for movement and contraction.

  • List and describe examples of globular proteins used for storage.

  • List and describe examples of globular proteins used for transport.

  • List and describe examples of globular proteins used as hormones.

  • List and describe examples of globular proteins used as receptors.

  • List and describe examples of globular proteins used in defense against disease.

  • List and describe examples of globular proteins used as enzymes.

  • Explain the role of mis-folded proteins in disease (specifically Alzheimer’s).

 

 

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Class Activities:

Interactome reading

Protein function notes

Amino acid packet

Protein memory match game

Protein structure notes

Unraveling the Mystery of Protein Folding

Modeling Protein Folding Lab

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Key Terms:

 

 

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Helpful Links:

 

 

   
   
"When we tug at a simple thing in nature, we find it attached to the rest of the world."  John Muir