Genetic Analysis: An Integrated Approach (3rd Edition)
3rd Edition
ISBN: 9780134605173
Author: Mark F. Sanders, John L. Bowman
Publisher: PEARSON
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Textbook Question
Chapter B, Problem 5P
Describe the gene and protein defects in phenylketonuria (PKU). How are these defects connected to disease symptoms?
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Discuss the potential difficulties of designing a diet to alleviate the symptoms of phenylketonuria.
Identify a disease or condition related to protein mis-folding. Which protein is misfolded? Is this a genetically inherited condition or is it transmissible?
Explain the genetic alterations resulting in protein synthesis defects and their relationship to disease processes such as sickle cell anemia and polycystic kidney disease.
Chapter B Solutions
Genetic Analysis: An Integrated Approach (3rd Edition)
Ch. B - Prob. 1PCh. B - Prob. 2PCh. B - B.3 Log on to the National Institute for Child...Ch. B - B.4 What communitybased genetic screening...Ch. B - B.5 Describe the gene and protein defects in...Ch. B - B.6 A couple and some of their relatives are...Ch. B - Prob. 7PCh. B - Do you think it is important that participation in...Ch. B - B.9 If a man and a woman are each heterozygous...Ch. B - B.10 Suppose a man and a woman are each...
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- Explain the reasons for the removal or reduction of nucleic acid in Single Cell Protein.arrow_forwardWhat are the 3 steps of amino acid degradation:arrow_forwardDiscuss protein folding and misfolding. Give two consequences (or examples) of protein misfolding and describe the effect of the misfolding.arrow_forward
- Which amino acid pair constitutes the hydrophobic patch on sickle cell hemoglobin that results in formation of protein oligomers with the Glu 6 --> Val 6 sickle cell mutation? Does normal hemoglobin contain this same amino acid pair constituting a hydrophobic patch? Phe 85 / Leu 88; no Phe 85 / Leu 88; yes Trp 85 / Leu 88; yes Olle 85 / Leu 88; yes Pro 85 / Lys 88; noarrow_forwardInsulin possesses two polypeptide chains denoted A and B that are linked by disulfide bonds. Upon denaturation by reduction of the SH groups of insulin, followed by reoxidation, only 7% of the hormone activity is recovered. This is the level of activity expected for random pairing of cysteine residues to form disulfide bonds. How can these data be reconciled with the hypothesis that the amino acid sequence directs protein folding?arrow_forwardA. Consider the dipeptideVal–Pro: What amino acid is the N terminal aminoacid? What amino acid is the C terminal aminoacid? How are the amino acids connected? Give the name of the dipeptide. Give the name of the dipeptide in which the amino acid order is reversed as Pro–Val.arrow_forward
- Describe the effect of the amino acid change on protein function: how does the HbS protein function differently than the HbA protein in red blood cells?arrow_forwardExplain the amino–imino forms of cytosine and adenine ?arrow_forwardIn TLC, why are the colors of the peaks for each amino acid are different depending on the types of amino acid?arrow_forward
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