1. The chains of several cell membrane-bound proteins wind back and forth through the cell membrane, such that some parts of the protein structure are extra-cellular, some parts are intra-cellular and some parts lie within the cell membrane. Do you think the primary structure of a protein can help in distinguishing the portions of a membrane protein embedded within the cell membrane from those that are not? Justify your answer.

1. The chains of several cell membrane-bound proteins wind back and forth through the cell membrane, such that some parts of the protein structure are extra-cellular, some parts are intra-cellular and some parts lie within the cell membrane. Do you think the primary structure of a protein can help in distinguishing the portions of a membrane protein embedded within the cell membrane from those that are not? Justify your answer.

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 2VCQ: Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble...

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3. Why do we need to study the four levels of protein structure? Cite its practical use to our day-to-day life.
1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric 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.
1. Describe how each of the following relates to protein configuration: primary structure - secondary structure - tertiary structure - quaternary structure -
7/ Hemoglobin is an example of a protein with A. Primary structure only. B. two protein chains held together. C. a quaternary structure. D. primarily a B-pleated sheet structure.
1. Explain how each primary structure of a protein affects its properties and how denaturation changes the structure. 2. Explain how each secondary structure of a protein affects its properties and how denaturation changes the structure.
2. Would you expect an instrinsically disordered protein to contain a higher proportion of hydrophilic or hydrophobic residues? Explain your reasoning.
1) What are the four levels of protein folding. How do you distinguish those different levels? What can denature a protein? 2) What are detergents and why are they useful? How do they basically work? 3) What is meant by amphipathic? What is an example of this?
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.
Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble protein, and which would you expect to find in the interior? What distribution of amino acids would you expect to find in a protein embedded in a lipid bilayer?
The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
1. To create a fully functional protein, how do their structure help in determining its function? 2. Discuss the reasons why proteins make up the largest percentage of a cell’s weight/mass? 3. How do the advent of bioinformatics help scientists understand the diversity of proteins?