Campbell Biology: Custom Edition
18th Edition
ISBN: 9781323717271
Author: Urry, Cain, Wasserman, Minorsky, Reece
Publisher: PEARSON C
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Chapter 14.4, Problem 2CC
Summary Introduction
To explain: The change in the single amino acid in hemoglobin that results in the aggregation of hemoglobin in long fibers.
Concept introduction:
The primary structure of proteins is the linear sequence of amino acids. It determines the shape and the functional ability of the protein. A small change in the amino acid sequence can alter a protein’s shape and its functions.
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Chapter 14 Solutions
Campbell Biology: Custom Edition
Ch. 14.1 - DRAW IT Pea plants heterozygous for flower...Ch. 14.1 - WHAT IF? List all gametes that could be made by a...Ch. 14.1 - MAKE CONNECTIONS In some pea plant crosses, the...Ch. 14.2 - Prob. 1CCCh. 14.2 - Two organisms, with genotypcs BbDD and BBDd, are...Ch. 14.2 - WHAT IF? Three characters (flower color, seed...Ch. 14.3 - What two properties, one structural and one...Ch. 14.3 - If a man with type AB blood marries a woman with...Ch. 14.3 - WHAT IF? A rooster with gray feathers and a hen...Ch. 14.4 - Beth and Tom each have a sibling with cystic...
Ch. 14.4 - Prob. 2CCCh. 14.4 - Prob. 3CCCh. 14.4 - MAKE CONNECTIONS In Table 14.1, note the...Ch. 14 - When Mendel did crosses of true-breeding purple-...Ch. 14 - DRAW IT Redraw the Punnett Square on The right...Ch. 14 - Inheritance patterns are often more complex than...Ch. 14 - Both members of a couple know that they are...Ch. 14 - DRAW IT Two pea plants heterozygous for the...Ch. 14 - A man with type A blood marries a woman with type...Ch. 14 - A man has six fingers on each hand and six toes on...Ch. 14 - DRAW IT A pea plant heterozygous for inflated pods...Ch. 14 - Flower position, stem length, and seed shape are...Ch. 14 - Hemochromatosis is an inherited disease caused by...Ch. 14 - The genotype of F1, individuals in a tetrahybrid...Ch. 14 - What is the probability that each of thc following...Ch. 14 - Prob. 9TYUCh. 14 - Prob. 10TYUCh. 14 - In tigers, a recessive allele of a particular gene...Ch. 14 - In maize (com) plants,a dominant allele I inhibits...Ch. 14 - The pedigree belowtraces the inheritance of...Ch. 14 - Imagine that you are a genetic counselor, and a...Ch. 14 - EVOLUTION CONNECTION Over the past half century,...Ch. 14 - SCIENTIFIC INQUIRY You are handed a mystery pea...Ch. 14 - Prob. 17TYUCh. 14 - SYNTHESIZE YOUR KNOWLEDGE Just for fun, imagine...
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- What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.arrow_forwardQ. In hemoglobin protein, an ion pair exists between lysine at position 40 (pka 10) and a beta-chain terminal carboxyl (pka 4). What fraction of these Lys-40/beta-carboxyl are actually in an ion pair at ph 7? а. О b. 0.1 C. 0.5 d. 0.9 е. 1.0arrow_forwardOne of the molecules listed below is effective in reducing O2 affinity of human Hb in the absence of BPG: (1) Glucose 6-phosphate (2) Inositol hexaphosphate (3) Maleic acid (4) Lactate (5) Arginine - Interestingly, this molecule plays the role of BPG in bird and turtle hemoglobin. A) Write the chemical structure of each molecule mentioned above. (B) Predict what molecule is most effective in preventing O2 binding to Hb. In 20 words or less explain the rationale for your predictionarrow_forward
- Give typed full explanationarrow_forwardIn an experiment, hemoglobin is dissociated in a buffer and a subunit is isolated to study for its oxygen binding affinity. (i) What is the shape of the oxygen dissociation curve is expected in the experiment?Explain why. (ii) Is the Km of the isolated subunit higher or lower than the Km of an intact hemoglobin?arrow_forwardHemoglobin from different species can have different numbers of subunits. Let's consider three hemoglobin molecules: n = 1, n = 4, and n = 8, where each subunit has an oxygen P50 = 30 torr. (Recall that Pso is essentially a Kp and that oxygen partial pressure (torr) is directly proportional to concentration.) Which molecule transports the most O2 between the lungs (pO2 = 100 torr) and peripheral tissues (pO2 = 30 torr)? Please justify your answer.arrow_forward
- The classic demonstration that cell plasma membranes are composed ofbilayers depends on the following kinds of data:• The membrane lipids from 4.74 x 109erythrocytes will form a monolayer of area 0.89 m2when spread on a water surface.• The surface of one erythrocyte is approximately 100 μm2in area. Show that these data can be accounted for only if the erythrocyte membrane is a bilayer.arrow_forwardApproximate P50 for myoglobin from its binding curve. Approximate P50 for normal hemoglobin and the hemoglobin mutant from the binding curve. At low pO2 (below 20 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant? At high pO2 (above 30 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant? Which protein, normal hemoglobin or the hemoglobin mutant, transports O2 more efficiently? Briefly explain your answer.arrow_forwardThe classic demonstration that cell plasma membranes are composed ofbilayers depends on the following kinds of data:• The membrane lipids from 4.74 x 109 erythrocytes will form a monolayerof area 0.89 m2 when spread on a water surface.• The surface of one erythrocyte is approximately 100 μm2 in area.Show that these data can be accounted for only if the erythrocyte membraneis a bilayer.arrow_forward
- What qualitative effect would you expect each of the following to have on the Ps0 of hemoglobin? (a) Increase in pH from 7.2 to 7.4 (b) Increase in Pco, from 20 to 40 mm Hg (c) Dissociation into monomer polypeptide chainsarrow_forwardThe primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.arrow_forwardWhy does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2arrow_forward
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