Genetics: From Genes to Genomes
6th Edition
ISBN: 9781259700903
Author: Leland Hartwell Dr., Michael L. Goldberg Professor Dr., Janice Fischer, Leroy Hood Dr.
Publisher: McGraw-Hill Education
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Chapter 1, Problem 12P
Figure 1.6 shows the amino acid sequences of parts of the cytochrome c proteins from several different organisms. Some of these amino acids are highlighted in dark orange, some in light orange, and some are not highlighted at all. Which of these three classes of amino acids is likely to be most important for the biochemical function of cytochrome c proteins?
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Chapter 1 Solutions
Genetics: From Genes to Genomes
Ch. 1 - Choose the phrase from the right column that best...Ch. 1 - If one strand of a DNA molecule has the base...Ch. 1 - The size of one copy of the human genome is...Ch. 1 - Indicate whether each of the following words or...Ch. 1 - a. How many different DNA strands composed of 100...Ch. 1 - RNA shares with proteins the ability to fold into...Ch. 1 - The human protein lactate dehydrogenase shown in...Ch. 1 - a. Are the triplets in the genetic code table...Ch. 1 - Why do scientists think that all forms of life on...Ch. 1 - Why would a geneticist study a yeast cell or a...
Ch. 1 - How can a scientist tell if a protein present in...Ch. 1 - Figure 1.6 shows the amino acid sequences of parts...Ch. 1 - Why do scientists think that new genes arise by...Ch. 1 - Explain how the exon/intron structure of genes...Ch. 1 - Mutations in genes that change their pattern of...Ch. 1 - A single zebrafish gene function was inactivated...Ch. 1 - Different mutations in the WDR62 gene that...Ch. 1 - Researchers have successfully used gene therapy to...Ch. 1 - By the time this book is published, it will likely...
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- To visualize the spatial arrangement of amino acid residues in an a-helix, it is helpful to imagine you are looking down the long axis of the helix, just as you would look down a soda straw. Viewed in this orientation, the residues form a circle, with each residue offset from its neighbor by 100 degrees. This representation is called a helical wheel. Use the circle below to indicate the position of each residue around the helix of the enzyme lysozyme. NH ...Arg - Cys - Glu- Leu - Ala Ala - Ala Met-Lys COO- The first two amino acids, Arg-1 and Cys-2, are shown as an example. Arg-1 O Glu-3 Which amino acid in the polypeptide is the first to pass the origin (i.e., which amino acid passes Arg- 1 first, completing one full circle)? Select the best answer. O Leu-4 O Ala-5 O Ala-6 O Ala-7 Met-8 O Lys-9 100° O none of the above Cys-2arrow_forwardSome of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.arrow_forwardLactose permease, a protein of E. coli, is composed of a singlepolypeptide that is 417 amino acids in length. By convention, theamino acids within a polypeptide are numbered from the aminoterminalend to the carboxyl-terminal end. Are the following questionsabout lactose permease true or false?A. Because the sixty-fourth amino acid is glycine and the sixty- eighth amino acid is aspartic acid, the codon for glycine,64, is closer to the 3′ end of the mRNA than the codon for aspartic acid, 68.B. The mRNA that encodes lactose permease must be greater than1241 nucleotides in length.arrow_forward
- A schematic diagram of the helical structure of cytochrome b562 is reproduced below. Thisprotein belongs to the family of -proteins that have a four-helix bundle. Number the helices 1 – 4according to their N C direction. Indicate relative orientations of the macrodipoles of helices 1 – 4adjacent to the diagram of cytochrome b562. Remember that according to the definition of a dipolethat the arrow points towards the positive end.arrow_forwardWhen performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?arrow_forwardFour proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. If the electrophoretic separation is carried out at pH 7.0, which protein would move toward the negative electrode? Cytochrome C Myoglobin Hemoglobinarrow_forward
- A seven-residue peptide was found to have an amino acid composition including glu, val, Lys, met, leu, and trp (there is more than one copy of one amino acid). Several reactions on samples of the peptide resulted in the following: a) Trypsin has no effect on the heptapeptide. b) If one cycle of Edman degradation provides the PTH derivative shown below, what does this tell you about the oligopeptide under investigation? [image] c) Chymotrypsin treatment yields a dipeptide, a tetrapeptide, and a free amino acid. Possibilities? d) The tetrapeptide contains val, lys, and met (only). What information does this give you? e) Cyanogen bromide treatment generates a dipeptide, a tetrapeptide, and free Lys. f)What is the sequence of the peptide?arrow_forwardIn each case, these are enzymes that catalyze thesame reaction in different species. The question is: are they related or not? i.e. Are the structures essentially the same? Often you can get similar reactions from proteins thatevolved from a common ancestor (e.g., trypsin and chymotrypsin). Sometimes the samereaction can be catalyzed by proteins with very different evolutionary origins and with verydifferent structures (e.g., trypsin and subtilisin). Your job is to decide if these proteins have fundamentally different folds or if they have basically the same fold. Briefly justify your answer.1. Aminopeptidases from a mammal (PR1A) and the malaria parasite (PR1B)2. Bisphosphoglycerate mutase from a mammal (PR2A) and the toxoplasma parasite(PR2B)arrow_forwardUsing the amino acid sequences in Cytochrome C provided in the following table, list the amino acid differences between a human and a selected animal; a. human and chicken = b. human and rabbit c. human and pony Animal Amino Acid Sequences in Cytochrome-c 1 234567 89 10 11 12 13 14 15 16 17 18 19 20 21 22 ain prophe thr thr ala ws asn lys thr lys olu olu thr leu met olu lys ala thr asn olu ain alu phe ser thr asp lys asn ys thr gly alu asp thr leu met glu lys ala thr ser lys gin ala phe ser thr asp lys asn lys thr aly glu asp thr leu met glu ser ala cys ser lys Human oln pro tyr ser the ala ys asn lve de olv alu asp thr leu met alu vs ala the asn alu oin gin phe ser thr asp vs ser lys thr aln gin olu the leu arg de ys thr ala ala ser ain pro tyr ser thr ala vs asn lys the oy olu asp thr leu met glu lys ala the asn olu oin val phe ser thr asp lys asn lys thr oly olu asp thr leu met olu lys ala thr asn oluarrow_forward
- Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of a glycoprotein. The saccharide is linked by a(1-2) linkages to three sialic acid residues, then O- linked to the glycoprotein. The glycoprotein is a glucose receptor. Running it through Benedict's Test produced negative results. What are 2 possible amino acids that is able to O-link with the saccharide? Show the part of both saccharide and protein where the bond is formed.arrow_forwardSelect the term in column B which best matches the description in column A. There are more terms then needed. Column A Column B 1. The pentose sugar found in DNA. a) Cis fatty acid b) Trans fatty acid c) Coenzyme d) Cofacipr 2. Commonly referred to as "insoluble fiber". 3. Considered to be an amphipathic molecule. 4. A molecule with the formula C18H3602 is probably a e) Phospholipid 5. Bond created during the formation of the primary structure of a protein. ) Glycogen 6. A non-protein organic molecule needed for proper enzyme functioning. g) Cellulose 7. Pyrimidine base found only in RNA. h) Galactose i) Fructose 8. Increasing the number of these molecules in the cell membrane would increase the permeability of the cell membrane. i) Thymine k) Uracil 9. Bond which connects nucleotide monomers together. 1) Fatty acid m) Disaccharide n) Peptide bond o) A-Helix p) B-Pleated Sheet q) Ribose r) Deoxyribose 10.arrow_forwardA spheroidal bacterium with a diameter of 1.0 μm (micrometer, 1 μm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?arrow_forward
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