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Week 3 Discussion Principles of CHemistry
Week 3 Discussion Principles of CHemistry
_________________________ _________________________
Spokesperson Reflector
THE PLAN: Our big overarching goal is to figure out how enzymes work in extreme environments. Last
week, we talked about how enzymes can impact reactions in the body by acting as a catalyst. Today we are
going to look further at how enzymes work. In this case, we are not going to look at just the active site but
expand this to look at protein folding and how that relates to entropy.
The learning objectives and skills for today’s session are for you to:
As explained in week 1, each member of the team will be assigned to a specific role, which will rotate each
week. The recorder should note who is performing each role in a given week. It is the responsibility of
all group members to double check that they are tagged on the Gradescope group submission and
that all pages of the correct document were uploaded to Gradescope before the deadline.
Recorder: Records answers for the team and submits the team report on Gradescope.
Reflector: Reads the questions and checks that the final conclusion makes sense and ensures that
all members have consistent answers.
Spokesperson: Presents answers (or questions) to the class, instructor, or other teams.
Manager: Keeps the team on task and on schedule. Considers how the team is working and how it
could improve in the future.
1. Briefly summarize what you learned about different levels of protein folding from the video.
2. a. Sketch a simple picture of both a folded and an unfolded protein. This can be represented as just
a line.
b. Thinking about your answer to question number 2a, which configuration do you expect to be
preferred? Justify your answer.
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3. Energetic factors focus on the potential energy of the substance due to interactions between
submicroscopic components (i.e., electrons, atoms, ions, molecules). For protein folding, this is
related to the intermolecular forces. What type or types of intermolecular forces are involved in
protein folding?
(HINT: This was discussed in Principles I and can be found in pages 195-196 of your textbook.)
5. Protein folding is largely influenced by the interaction of the R-groups (side chains) with the
environment. Explain how this interaction relates to the polarity of the R-groups. How does the
fact that the proteins must fold in certain ways because of these interactions affect the number of
configurations available to the protein?
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6. We also have to think about entropic factors when we think about thermodynamic stability.
Entropic factors influence the number of different configurations in which submicroscopic
components of the substance may exist. Think about your answer to question 5 – Does protein
folding increase or decrease entropy? Justify your answer.
7. Consider the role of energetic and entropic factors for protein folding.
a. Draw a PEC diagram that represents the relative potential energy and number of
configurations for the unfolded and folded protein.
b. Explain which factor(s) provide the driving force(s) for protein folding.
REFLECTING ON SKILLS
An important part of developing skills that are important for supporting your learning (and that are highly
valued by employers) is to assess your progress and identify areas where you can improve.
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Indicate the number on the rubric you think best characterizes your level of acting as a cohesive unit today.
Why did you give your team this rating? Provide specific evidence related to your interactions an observer
would have seen to support this rating.
What is one way you can improve your performance next week? How do you plan to achieve this?
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CONTINUING ON ...
8. Open the simulation on protein folding found on page 201of your textbook
https://lab.concord.org/embeddable.html#interactives/samples/5-amino-acids.json
Notice that you can change both the solvent type and the hydrophobicity of the protein. Change the
settings to “all hydrophobic.”
a. Before running the simulation, predict what you think will happen to the protein if you set the
solvent to water and provide a justification.
b. Run the simulation to see if you were correct. Was your initial prediction correct?
9. Now change the simulation settings to water and mostly hydrophilic amino acids.
a. How does this change the protein folding process?
10. Looking at the simulation, how do you think that the hydrophobicity/hydrophilicity of the amino acids
in an aqueous solution impacts the entropic factors?