OL Lab 2: Protein Denaturation
Learning Objectives:
• Understand how protein denaturation.
• Understand how interactions between side groups influence the protein structure
• Understand the chemical and physical ca
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OL Lab 2: Protein Denaturation
Learning Objectives:
• Understand how protein denaturation.
• Understand how interactions between side groups influence the protein structure
• Understand the chemical and physical causes of protein denaturation
• Understand the results of protein denaturation
Introduction:
Proteins are one of the major biomolecules in the body. It has to maintain its proper shape and structure for it to be functional biomolecule. Protein’s structure can be disrupted due to many factors. In this simulation you will explore how chemical and physical factors cause protein denaturation. You will perform various experiments using ovalbumin, the primary protein found in eggs, in order to understand the chemical and physical causes of protein denaturation. Will you be able to unravel the factors that affect a protein molecule?
Part 1: Complete Labster Protein Denaturation Part 2: Report and Reflection
Purpose: Describe in your own words and in complete sentences, the purpose of this experiment.
The purpose of this lab was to gain the understanding of what protein denaturing is and its results. The lab also helped us understand interactions between side groups affect the protein structure.
Observations: List 3 observations you have made in this simulation.
Some observations that I made during this experiment was how temperature and pH affect a protein. If the enzyme and substrate are exposed to a non-optimal environment, say too hot or too drastic pH change, weak bonds can be broken causing the active site of the substrate or the enzyme shape itself to change form or become "denatured" thus they cannot bond together to drive the reaction. Another observation that I made during the lab was when we were testing different kinds of chemicals to see how they react in the solution.
Answer all the questions below:
1. List out four abundant elements found in the body and state their contribution to body functions. (2 points)
The four most abundant elements in the human body hydrogen, oxygen, carbon, and nitrogen account for more than 99 per cent of the atoms inside you. They are found throughout your body, mostly as water but also as components of biomolecules such as proteins, fats, DNA, and carbohydrates.
2. How does the protein shape determine its function? (1 point)
Protein has its own unique sequence of amino acids and how its interactions between these amino acids create a specify shape.
3. What are enzymes and how does pH and temperature affect enzymatic activity? (3 points)
An enzyme is a protein found within a cell. Enzymes create chemical reactions in the body and work best within specific temperature and pH ranges, but outside those parameters can cause an enzyme to lose its ability to bind to a substrate. Raising temperature generally speeds up a reaction, and lowering temperature slows down a reaction. Extreme pH values can cause enzymes to denature.
4. List 3 enzymes that function at different pH in our body. (3 points)
Enzymes are sensitive to pH which can change the active site because many amino acids in an enzyme carry a charge. Salivary Amylase functions at an optimum pH of 6.8. Stomach Protease (pepsin) functions at an optimum pH of 1.5-2.0. Pancreatic Protease (trypsin) functions at an optimum pH of 7.5-8.0.
5. Reflection: Reflect on at least 2 key concepts you have learned from this simulation. How would you relate it to the physiological functions of the body? One key concept that I learned during the lab is how acid denatures protein by modifying the pH and disrupting the salt bridges. Another key concept that I learned during the lab is how heat affects a way a protein is denatured. Heat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted. When a protein is denatured, secondary and tertiary structures are altered but the peptide bonds of the primary structure between the amino acids are left intact. Since all structural levels of the protein determine its function, the protein can no longer perform its function once it has been denatured.
Grading Rubric:
Activity
Deliverable
Points
Part 1
Complete simulation
15
Part 2
Complete lab report and answer questions
• Purpose (1 point)
• Observation (3 points)
• Questions (9 points)
• Reflection (2 points)
15
Total
Complete all lab activities
30
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