3 Shown below is the structure of a protein:From this structure, what is the predominant secondary structure of the protein?Based on what you can observe from the protein, what is its highest level of organizational structure?If applicable, how many subunits does this protein have and are they identical?If electrostatic interactions primarily stabilize this structure, propose a method to test your observations in 4.2 and 4.3.

Lindsay-Lang proposed the first protein structural hierarchy with four levels: Central, secondary,…

Answered: 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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Similar questions

Hemoglobin is a tetramer consisting of two a and two b chains. What level of protein structure is described in the above statement?
Hemoglobin is a tetramer consisting of two α and two β chains.What level of protein structure is described in this statement?
Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?
In regards to the protein structure, explain what is meant by “tertiary structure.” Whatare the main forces that stabilize tertiary structures in proteins? Provide examples.
What are the four levels of protein structure/ organization and what types of bonds are involved in each?
Proteins are polymers of amino acids that fold in which three dimensions?
In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains. Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.
What are the four levels of protein structure, and what is the distinguishing feature of each?
For the protein given in the attached picture: Write the name of these 5 amino acids corresponding to their abbreviation of 3 letters. Describe precisely how the functional groups in the amino acids are involved in bonding between two successive amino acids in the protein.
Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.
At what level of protein structure do multiple polypeptide chains interact?
At what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.

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