Four Levels of Protein Structure (SAM) (a 9-page 1-2 day activity)

Interactive, scaffolded model

Overview and Learning Objectives

Students explore the four levels of protein folding. They explore variations of surface charges of amino acids and correlate them to the structure of the proteins they form.

Students interpret how the sequence and properties of amino acids relate to how proteins fold. They identify patterns of folding known as secondary structure and explore final folding patterns. Finally, students learn about how tertiary and quaternary structure relate to protein function.

Students will be able to:

• Recognize that a protein’s three‐dimensional shape allows it to perform a specific task.

• Identify the primary structure of a protein as a linear sequence of amino acids.

• Identify the unique side chains of amino acids that give them their properties.

• Explore how amino acids interact with water and how that affects the way

proteins fold.

• Differentiate among the common secondary structures of a protein and identify the importance of hydrogen bonding in stabilizing these structures.

• Identify tertiary structure as the final folding pattern of a protein and infer that

mistakes in folding are responsible for many human diseases.

• Explain that quaternary structure occurs when a protein is composed of more than one subunit, and that the subunits form a complex to achieve functionality.

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Central Concepts

Key Concept:

Additional Related Concepts

Molecular Biology

• Primary structure
• Protein Folding
• Protein Function
• Protein structure
• Self-assembly

Systems

• Emergent Properties

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Benchmarks and Standards

NSES

• Life Science: The Cell - 1 Cells have particular structures that underlie their functions (Full Text of Standard)
  
  
• Life Science: The Cell - 3 Cells store and use information to guide their functions (Full Text of Standard)
  
  

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Activity Credits

Created by CC Project: SAM using Molecular Workbench

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