Principles of Biology
2nd Edition
ISBN: 9781259875120
Author: Robert Brooker, Eric P. Widmaier Dr., Linda Graham Dr. Ph.D., Peter Stiling Dr. Ph.D.
Publisher: McGraw-Hill Education
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Chapter 5.3, Problem 1BC
Summary Introduction
To determine:
The amino acid, out of leucine or lysine that is expected to cross an artificial membrane more quickly.
Introduction:
The movement of a substance from a region of high concentration to a region of low concentration is termed as diffusion. The diffusion of some substance takes place across the plasma membrane, and the rate of the diffusion may be affected by some factors.
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Assume that the number of different types of bases in RNA is four. What would be the minimum codon size (number of nucleotides) required to specify all amino acids if the number of different types of amino acids in proteins were (a) 2, (b) 8, (c) 17, (d) 45, (e) 75?
Consider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary) as defined for proteins. (a) What level is shown by doublestranded DNA? (b) What level is shown by tRNA? (c) What level is shown by mRNA?
1) what is the net charge of the amino acid leucine of it is on the C-terminus end and why?
2) if the amino acid was changed to lysine on the c-terminus end explain why and what the net charge would be?.
Chapter 5 Solutions
Principles of Biology
Ch. 5.1 - Which of the following is not a characteristic of...Ch. 5.1 - Prob. 2TYKCh. 5.2 - In an animal cell, how can changes in lipid...Ch. 5.2 - Prob. 2CCCh. 5.2 - Prob. 1TYKCh. 5.2 - Which of the following changes would make a...Ch. 5.3 - Prob. 1BCCh. 5.3 - Prob. 1CCCh. 5.3 - Prob. 2BCCh. 5.3 - Prob. 2CC
Ch. 5.3 - Prob. 1TYKCh. 5.3 - Prob. 2TYKCh. 5.4 - Prob. 1CCCh. 5.4 - Prob. 1TYKCh. 5.4 - Prob. 2TYKCh. 5.5 - Prob. 1BCCh. 5.5 - Prob. 1TYKCh. 5.6 - Prob. 1CCCh. 5.6 - A form of endocytosis that involves the formation...Ch. 5.7 - Prob. 1CCCh. 5.7 - Prob. 2CCCh. 5.7 - Prob. 1BCCh. 5.7 - Anchoring junctions that adhere adjacent animal...Ch. 5 - Which of the following statements best describes...Ch. 5 - Which of the following events in a biological...Ch. 5 - Prob. 3TYCh. 5 - Carbohydrates of the plasma membrane are bonded to...Ch. 5 - Which of the following movements would not be an...Ch. 5 - Prob. 6TYCh. 5 - Prob. 7TYCh. 5 - What features of a membrane are a major...Ch. 5 - Prob. 9TYCh. 5 - Large particles can be brought into the cell by...Ch. 5 - With your textbook closed, draw and describe the...Ch. 5 - Describe two different ways that integral membrane...Ch. 5 - A principle of biology is that living organisms...Ch. 5 - Prob. 1CBQCh. 5 - With regard to bringing solutes into the cell...
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- The protein shown here is flavodoxin, which contains both alpha helices and beta sheets.arrow_forwardA cell has a defective enzyme that attaches the alanine amino acid (Ala), instead of a valine amino acid (Val), to tRNAs with the anticodon CAA. Will any polypeptides in the cell contain valine? Why or why not?arrow_forwardConsider a short peptide that forms an alpha-helix within a larger protein structure. Suppose that one glutamate residue at some specific position in the helix were mutated to a leucine residue. The mutation could either make the helix more stable, or less stable. i) Describe two situations in which a Glu-to-Leu mutation could make the helix more stable. ii) Describe two situations in which the Glu-to-Leu mutation could make the helix less stable. Explain briefly the basis for the stabilizing and destabilizing effect in all cases.arrow_forward
- Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?arrow_forwardWhich amino acid replacement would result in the biggest structural change in a protein if a Cys residue was replaced with Ser or Phe amino acid, and why?arrow_forwardShown below are two cartoon views of the small globular protein StrepG inwhich an α helix is packed against a four-strand β sheet. The sheet is madeup of two “β-hairpins” (a β-hairpin is a “β-turn-β” structure). Refer to theimages and answer the questions that follow: (a) Identify the locations of the N- and C-termini of StrepG.(b) Indicate the orientation of the helical macrodipole, showing the (δ+)and (δ-) ends of the macrodipole.(c) How many residues are in the helix?(d) Do you predict that the α helix and β sheet are amphiphilic or not?Briefly explain.(e) The following two peptides are part of the primary sequence of StrepG.Based on your answer to part (d), which one is more likely to correspondto the α helix? Which is most likely to be part of a β-hairpin? Explainyour choice.Peptide #1: DAATAEKVFKQYAND or Peptide #2: VDGEWTYDDATKTFTVarrow_forward
- An American biochemist Erwin Chargaff discovered that in the cells of all organisms he studied, the amount of adenine is always equal to the amount of thymine, and the amount of cytosine is always equal to the amount of guanine. Explain his findings.arrow_forwardThe infectious prion protein which are believed to cause a neurodegenerative disease by acting as a template to misfold other cellular prion proteins are usually β-helices. Is this correct or not?arrow_forwardWhy new peptides always grow at their C-terminal ends in translation (The same question can be phrased as “why peptide elongation in translation always happens in the N-terminal-to-C-terminal direction”)?arrow_forward
- Consider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why notarrow_forwardThe following questions refer to the peptide with a sequence of: Asp-Ser-Lys-Asn-Glu a) Would you expect this peptide to be soluble in water? Why or why not?arrow_forwardTo 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_forward
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