. Consider a base substitution mutation that occurred in a DNA sequence that resulted in a change in theencoded protein from the amino acid glutamic acid to aspartic acid. Normally the glutamic acid amino acidis located on the outside of the soluble protein but not near an active site.O-H¨A. What type of mutation occurred?O-HB. What 2 types of chemical bonds are found in the R-groupsof each amino acid? The R groups are shaded.CH2CH2CH2H2N-C-COOHH2N-C-COOH1HGlutamic acidHAspartic acidC. What 2 types of bonds could each R-group of each of these amino acids form with other molecules?D. Consider the chemical properties of the two amino acids and the location of the amino acid in theprotein. Explain what effect this mutation will have on this protein's function and why.

The mutation described is a base substitution that changes glutamic acid to aspartic acid in a…

Answered: . Consider a base substitution mutation…

Biology Today and Tomorrow without Physiology (MindTap Course List)

5th Edition

ISBN:9781305117396

Author:Cecie Starr, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Christine Evers, Lisa Starr

Chapter7: Gene Expression And Control

Section: Chapter Questions

Problem 2CT

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Which of the following is a functional group that is part of a building block of proteins? phosphate adenine amino ribose
Explain what happens if even one amino acid is substituted for another in a polypeptide chain. Provide a specific example.
Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
Explain what happens if even one amino acid is substituted for another in a polypeptide chain. Provide a specific example.
Amino acids have the generic structure seen below, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.
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.
a. Can a mutation change a proteins tertiary structure without changing its primary structure? b. Can a mutation change a proteins primary structure without affecting its secondary structure?
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
VISUALIZE Sketch a pyrimidine nucleotide subunit that would be found only in RNA. Circle and label the three components that make up this type of nucleotide. Explain what changes in the functional groups of this subunit would have to occur for it to be found in a DNA molecule.
Mad cow disease is an infectious disease where one misfolded protein causes all other copies of the protein to being misfolding. This is an example of a disease impacting structure. primary secondary tertiary quaternary

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