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.

Hi! Since you have posted multiple questions and have not mentioned which to answer, we will answer…

Answered: 5. Protein folding is largely…

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

See similar textbooks

Similar questions

17. Protein folding results in a large decrease in entropy since a polypeptide is now constrained and more ordered. However, what counterbalances the loss of entropy associated with protein folding?
2. 3. Where in your cell can you find the instructions for how to make all of the proteins?*
29. In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the structural levels of the protein modified?
4. Let’s build a polypeptide chain a. Using your arsenal of 4 amino acids, write out the primary structure of an 8 amino acid long polypeptide that you might be called amphipathic and thus allow it to form a micelle in aqueous solution, identify amino acid 1 through 8 as well as the location of the amino and carboxy termini of the polypeptide. b. Explain why this polypeptide would be considered amphipathic and draw what the micelle might look like in water. c. Taking amino acids 3, 4, and 5, draw the molecular structure of this particular stretch of polypeptide chain. Along the backbone linkage of the polypeptide identify the peptide bonds with a PB, the bonds with free rotation FR, and bonds with limited rotation LR.
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
. Theoretical and experimental measurements show that in many cases, the contributions of ionic and hydrogen-bonding interactions to AH for protein folding are close to zero. Provide an explanation for this result.,
3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule
4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
20. The dissociation constant of protein Z for ligand Y is: 10 micromolar. What fraction of the ligand is bound at ligand concentration = 5 micromolar?
3. One of the 20 standard amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? What is its three-letter abbreviation and one-letter code? Write the chemical structure of this amino acid at physiological pH.
4. What type of tertiary structure interactions are most likely between the following amino acids? (Use a reference chart as necessary.) (b) methionine and methionine (a) glycine and valine (d) serine and lysine (c) cysteine and cysteine

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS