Using a biochemical technique called site-directed mutagenesis, it is possible to substitute a specific amino acid residue in a protein with another amino acid residue. Which of the following substitutions would affect the protein's structure the least? a. Asp replaced by Glu b. Asp replaced by Thr c. Asp replaced by Ala d. Asp replaced by Asn

Using a biochemical technique called site-directed mutagenesis, it is possible to substitute a specific amino acid residue in a protein with another amino acid residue. Which of the following substitutions would affect the protein's structure the least? a. Asp replaced by Glu b. Asp replaced by Thr c. Asp replaced by Ala d. Asp replaced by Asn

Name: Using a biochemical technique called site-directed mutagenesis, it is
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Description: Using a biochemical technique called site-directed mutagenesis, it is possible to substitute a specific amino acid residue in a protein with another amino acid residue. Which of the following substitutions would affect the protein's structure the lea

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter11: Genome Alterations: Mutation And Epigenetics

Section: Chapter Questions

Problem 14QP: In the gene-coding sequence shown here, which of the following events will produce a frameshift...

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You are a molecular biologist studying a defective human protein that is known to be the cause of a rare cancer. You isolate the suspected protein from a person with this cancer and compare it to the same protein in a person without the cancer. You discover that the protein isolated from the cancer patient is slightly smaller in size when compared to the protein from the unaffected patient. Furthermore, you discover that the protein from the cancer patient differs in almost every amino acid starting after the twenty-third amino acid. What is the likely explanation?
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You are a molecular biologist studying a defective human protein that is known to be a cause of a rare cancer. You isolate the suspected protein from a person with this cancer and compare it to the same protein in a person without the cancer. You discover that the protein isolated from the cancer patient is slightly smaller in size when compared to the protein from the unaffected patient. Furthermore, you discover that the protein from the cancer patient differs in almost every amino acid starting after the 23rd amino acid. What is the likely explanation?
Which of the following describe how the order of nucleotide bases along a gene in the DNA ultimately determines the primary structure of a protein and how the primary structure ultimately determines the three-dimensional shape and function of the protein coded for by that gene. A Certain amino acids in a protein interact with other amino acids in that same protein and so the order of amino acids ultimately determines the 3-dimensional tertiary structure of that protein. B The order of nucleotide bases along the DNA is transcribed into complementary tRNA which is translated into the correct amino acid sequence for the protein by mRNA. C The order of nucleotide bases along a gene determines the order of amino acids in the resulting protein. The order of amino acids in the protein is called its secondary structure.
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