5. Protein folding is largely influenced by the interaction of the R-groups (side chains) with theenvironment. Explain how this interaction relates to the polarity of the R-groups. How does thefact that the proteins must fold in certain ways because of these interactions affect the number ofconfigurations 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 submicroscopiccomponents of the substance may exist. Think about your answer to question 5 - Does proteinfolding 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 aline.a. Thinking about your answer to question number one, which configuration do you expect tobe preferred? Justify your answer.

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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?

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 7TYK: In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme...

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2 If a protein is predominantly made up of aliphatic and aromatic amino acids, which of the following is most likely true about such protein? Select the correct responses): a. It is a protein with a net negative charge b. It is most probably a structural protein. c. It is a protein that is cationic in nature. d. It is a protein that is hydrophobic in nature. e. It is most probably a catalytic protein. f. It is a water-solube protein. g. It is most probably a carrier protein.
1. Regarding proteins, what is meant by the following terms? A. Zwitterion B. pI C. Isoelectric point D. denaturation E. Catalyst F. Cofactor G. Coenzyme 1a. Why are proteins catalysts known as enzymes necessary to sustain life processes? 1b. Describe the interaction between enzyme and its substrate.
1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation
8. A dipeptide T, obtained from the breakdown of an enzyme found in the human body, is made up of Amino Acids R and S. (a) Classify Amino Acids R and S as an acidic amino acid or a basic amino acid. (b) Name Bond Q. (c) State any ONE type of protein that could be found in human body. (2%) (1%) (1%)
In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activation
The assembly of proteins from amino acids is best described as: a. a conversion of kinetic energy to potential energy reaction. b. an entropy reaction. c. a catabolic reaction. d. an anabolic reaction. e. an energy-free reaction.
Which of the following analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces
1. If a molecule is interating with its side chains of an enzymes active site but it is not the substrate of the enzyme what kind of enzyme regulation is this? 2. What is the change in thetype of bond between Ser 80 -> Arg. 3. Will this change cause the complex to be more or less stable. Explain
2. a. How do the majority of proteins that exist outside cells get outside cells? Explain the pathway. b. Explain at least three major exceptions to your answer in part a.
2. Explain in molecular terms why humans cannot use cellulose as a nutrient, but goats and cattle can.
1. What are the effects of a) amino acid composition and sequence and b) intramolecular and intermolecular forces of attraction to protein folding? 2. What molecular property of amino acids can be used to justity the concept that the "molecular part of the protein can exhibit the same property as the molecular 'whole' (protein molecule?). Provide a comprehensive discussion using one molecular property. 3. Discuss two metabolic disorders which are caused by protein misfolding. Explain the metabolic consequence of the disorder. 4. If a non-science person asks you what protein folding is and how the concept is related to metabolic disorders, how are you going to explain the concept? (please summarize the concepts used, thank you!)