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?
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?
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Transcribed Image Text: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?
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.
2. Sketch a simple picture of both a folded and an unfolded protein. This can be represented as just a
line.
a. Thinking about your answer to question number one, which configuration do you expect to
be preferred? Justify your answer.
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