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Ch.3 - Protein Structure and Function
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All textbooksFreeman 8th EditionCh.3 - Protein Structure and FunctionProblem 3

Chapter 3, Problem 3

What type of information is used to direct different polypeptides to fold into different shapes?

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Hello everyone. And in today's video we have a rather short problem. So let's jump straight into it. So which of the following? Irresponsible for altering the structure and function of a protein. So we're giving sort of answer choices such as the length, the sequence and the weight of the amino assets. And we need to select which one. So I want you to recall what a protein is and it's just a higher structure that is made up of just a sequence of amino acids. So let's visualize that now the sequence of amino acid is what essentially makes up this protein. If we have this sequence let's call it protein one. However, if we change this sequence of amino acids, let's say that we have B. A C. D. We do not have protein one anymore. We're gonna have protein too. And this protein two is going to have a different structure and function as protein one because it has a different sequence of amino acids that make it up because of this answer choice B The sequence of the amino acids that make up the protein is the only thing among our answer choices that is going to affect the structure and the function of set proteins. That's going to be the final answer to her question. I hope this video helped
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Related Practice
Textbook Question

What two functional groups are bound to the central carbon of every free amino acid monomer?


a. an R-group and a hydroxyl group

b. an amino group and a hydroxyl group

c. an amino group and a carboxyl group

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Textbook Question

What are the defining characteristics of a condensation reaction? a. Two monomers are covalently bonded together and a water molecule is produced. b. Two monomers are covalently bonded together and a water molecule is used up. c. A polymer is broken down into monomers and a water molecule is produced. d. A polymer is broken down into monomers and a water molecule is used up.

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Textbook Question

What type of bond is directly involved in the formation of an α-helix? a. peptide bonds between amino acid residues b. hydrogen bonds between amino acid residues c. van der Waals interactions between nonpolar residues d. disulfide bonds between cysteine residues

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Textbook Question

If a cell were to use only 10 of the 20 possible amino acids, how much effect would you expect this to have on protein diversity? Calculate and compare the number of different sequences that can be generated by randomly assembling either 10 or 20 amino acids into peptides that are five residues long.

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Textbook Question

Explain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.

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Textbook Question

Why are proteins not considered to be a good candidate for the first living molecule? a. Their catalytic capability is not sufficient for most biological reactions. b. Their amino acid monomers were not likely present in the prebiotic soup. c. They cannot serve as a template for replication. d. They could not have polymerized from amino acid monomers under early Earth conditions.

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