hi please answer all and i'll give you like 4.1. From this structure, what is the predominant secondary structure of the protein?4.2. Based on what you can observe from the protein, what is its highest level of organizational structure? (-4.3. If applicable, how many subunits does this protein have and are they identical? (4.4. If electrostatic interactions primarily stabilize this structure, propose a method to test your observationsin 4.2 and 4.3.

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Answered: 4.1. From this structure, what is the…

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter2: Chemistry Of Life

Section: Chapter Questions

Problem 7RQ: Describe the four levels of protein structure. How do a proteins side groups influence its...

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4.1. From this structure, what is the predominant secondary structure of the protein? 4.2. Based on what you can observe from the protein, what is its highest level of organizational structure? 4.3. If applicable, how many subunits does this protein have and are they identical? 4.4. If electrostatic interactions primarily stabilize this structure, propose a method to test your observations in 4.2 and 4.3. I
3
If the protein you are studying is known to bind the molecule shown below, what types of amino acids would you expect to be forming interactions at each of the numbered positions. Explain your reasoning for your choices 2 0 N* H- H H. 4. 3. 1,
9. A) Please write down the names of the following protein folds. A B C B) Which one(s) is made of more than one polypeptide? D E 000 C) Give an example of a protein containing the motif in C and explain how the structure of this motif facilitates function. 10. What is Levinthal's paradox? Describe the paradox and explain the conclusion to which it led.
X2.36.1
15,2
How do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could giverise to each interaction.(a) Hydrophobic interactions(b) Salt bridges (ionic interactions)
How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.(a) Side-chain hydrogen bonding(b) Disulfide bonds
Among the many different biological functions of proteins, identify and describe two (2) general functions. Explain how theprotein structure relates to these functions. Cite a particular protein that exhibits each function you have described and give the unique features of its primary, secondary, tertiary, and quaternary (if applicable) structures.
18.1
Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)
Consider a small protein containing 101 amino acid residues. The proteinbackbone will have 200 bonds about which rotation can occur. Assume thatthree orientations are possible about each of these bonds.(a) Based on these assumptions, about how many random-coil conformationswill be possible for this protein?(b) The estimate obtained in (a) is surely too large. Give one reason why.

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