Campbell Biology In Focus, Loose-leaf Edition (3rd Edition)
3rd Edition
ISBN: 9780134895727
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky
Publisher: PEARSON
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Chapter 21, Problem 8TYU
Summary Introduction
To explain:
How cellular and molecular events are responsible for emergent properties at individual and population level.
Introduction:
The events taking place at molecular or cellular level can lead to emergent properties at individual level or population level. The heterozygote alleles are favored rather than homozygotes at cellular level. In humans, this advantage can be seen at a locus coding for ß polypeptide (subunit of hemoglobin).
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Hemoglobin is a complex protein that contains four polypeptide chains. The normal hemoglobin found in adults—called adult hemoglobin— consists of two alpha and two beta polypeptide chains, which are encoded by different loci. Sickle-cell hemoglobin, which causes sicklecell anemia, arises from a mutation in the beta chain of adult hemoglobin. Adult hemoglobin and sickle-cell hemoglobin differ in a single amino acid: the sixth amino acid from one end in adult hemoglobin is glutamic acid, whereas sickle-cell hemoglobin has valine at this position. After consulting the genetic code provided in Figure 15.10, indicate the type and location of the mutation that gave rise tosickle-cell anemia.
Given below is the electrophoretic profile of 2 proteins,
a normal hemoglobin, HbA and the fetal hemoglobin,
HbF. What information can be obtained from the profile
shown?
wwwwwww
(+)
HbF
ww w
(-)
HbA
ww ww
A. HbF has a slightly different conformation compared with
HbA
B. HbF and HbA have different primary structures
C. HbF has a higher affinity for oxygen than HbA
D. HbF has a nonpolar amino acid residue in place of a basic
amino acid.
E. HbF has an acidic amino acid residue in place of a
nonpolar amino acid
Sickle-cell anemia is a genetic disorder of individuals homozygous for a mutation of hemoglobin that causes their red blood cells to be sickle shaped and stiff under conditions of low pO2. Why is this disease life threatening?
Chapter 21 Solutions
Campbell Biology In Focus, Loose-leaf Edition (3rd Edition)
Ch. 21.1 - Explain why genetic variation within a population...Ch. 21.1 - Of all the mutations that occur in a population,...Ch. 21.1 - Prob. 3CCCh. 21.2 - A population has 700 individuals, 85 of genotype...Ch. 21.2 - The frequency of allele a is 0.45 for a population...Ch. 21.2 - WHAT IF? A locus that affects susceptibility to a...Ch. 21.3 - In what sense is natural selection more...Ch. 21.3 - Distinguish genetic drift from gene flow in terms...Ch. 21.3 - WHAT IF? Suppose two plant populations exchange...Ch. 21.4 - What is the relative fitness of a sterile mule?...
Ch. 21.4 - Explain why natural selection is the only...Ch. 21.4 - Consider a population in which heterozygotes at a...Ch. 21 - Natural selection changes allele frequencies...Ch. 21 - Sparrows With average-sized w1ngs survive severe...Ch. 21 - If the nucleotide variability of a locus equals...Ch. 21 - There are 25 individuals in population 1, all with...Ch. 21 - A fruit fly population has a gene with two...Ch. 21 - FOCUS ON EVOLUTION Using at least TWO examples,...Ch. 21 - Prob. 8TYUCh. 21 - SYNTHESIZE YOUR KNOWLEDGE This kettle lake formed...
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- A genetic variant of the HBB gene results in sickle cell anemia, a disorder than primarily affects people of Sub-Saharan African descent, including many black Americans. Sickle cell anemia is named after the shape of the red blood cells in individuals with this disorder. The diseased genetic variant in the HBB gene results in a malformed hemoglobin protein, which is responsible for the shape of the red blood cell. Patients diagnosed with this disorder often exhibit a variety of symptoms, such as episodes of pain, swelling of hands and feet, delayed growth, and vision problems amongst others. The malformed hemoglobin protein is an example of the relationship between genes and traits at the: molecular level. population level. cellular level. organism level.arrow_forwardOne molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).arrow_forwardHemoglobin is composed of how many polypeptide chains thatchange during development?arrow_forward
- Sickle cell anemia patients suffer from a distorted red blood cell shape and an anemic condition as a result of a genetic mutation in the HBB gene, which codes for the hemoglobin β subunits. This mutation changes a Glu to a Val at position 6 in the protein, and these patients express two alleles (one from each parent) with this mutation. When individuals inherit just one copy of this mutated gene, they are considered carriers, and have very few symptoms. Based on the quaternary structure of hemoglobin, what can you predict about the assembly of hemoglobin in sickle cell anemia patients versus carriers of the sickle cell trait? a. In sickle cell anemia patients, the α globin subunits have complementary mutations to ensure the quaternary structure of hemoglobin is attained. b. In sickle cell anemia patients, 100% of the hemoglobin is fully functional, whereas in those that carry the trait, there is no functional hemoglobin assembled. c. In individuals with the sickle cell…arrow_forwardA red heme-containing protein called leghemoglobin is found in the nitrogen-fixing root nodules of leguminous plants. The protein component is produced by the plant, whereas bacterial cells produce the precursor of heme. Can you deduce the function of leghemoglobin? [Hint: Leghemoglobin is a member of the globin superfamily.]arrow_forward4. You are to choose the members of an expedition that will climb several high mountains. Each applicant for one of the positions is a heterozygote for an abnormal hemoglobin: Person A: Hb Albany: a methionine has been substituted for Lys 82 in the B-subunit. Person B: Hb Cowtown: a leucine has been substituted for His 146 in the B-subunit. Person C: Hb Flagstaff: an isoleucine has been substituted for Val 1 in the B-subunit. For the locations of the amino acid residues refer to your text, the figure on page 9 of this lab, and the KING exercises. Assuming that each of these candidates is equal in ability at low altitude, which one would you choose for the expedition? To answer this question, determine how the substituted amino acid affects the structure and function of each abnormal hemoglobin, and describe the physiological effect. Focus on the stabilization of the T versus R state of hemoglobin, and the consequent physiological changes that might occur altitude. Keep your answers…arrow_forward
- One of your patients, a six-year-old girl who suffers from Sickle cell anemia, an inherited blood disorder in which red blood cells are abnormally shaped and fragile, leading to a short supply of red blood cells. These abnormal cells can also get stuck in small vessels, which prevent blood flow, leading to fatigue, pain, and other severe complications. Patients with sickle cell anemia produce defective beta-globin due to a point mutation that causes the change of a single amino acid residue. This is an example of what type of mutation? nonsense mutation missense mutation frameshift mutation deletion mutationarrow_forwardThere is a benign congenital condition called Hereditary Persistence of Fetal Hemoglobin (HPFH) in which production of the fetal hemoglobin (HbF) is not switched off post-partum (after birth). It is due to a mutation in the β-globin gene cluster. People that are homozygotes for this mutation, meaning that the gene from both parents is mutated, continue to make almost exclusively HbF throughout their life rather than adult hemoglobin (HbA). HPFH homozygotes demonstrate a slight erythrocytosis, or an increase in the number or mass of their red blood cells, and consequently an increase in the concentration of HbF. Given only what you know about the oxygen saturation dynamics of HbF versus HbA, can you explain why there might be the slight erythrocytosis in HPFH homozygotes? It has been observed that the prevalence of HPFH is much higher in populations with certain hemoglobinopathic disorders such as sickle cell anemia, and is selected for in populations with a high prevalence of these…arrow_forwardsickle hemoglobin when deoxygenated will create a long line of protein cells? is this true? Please explain your answer. thanksarrow_forward
- Normal Hgb is referred to as HbA and contains 4 subunits, 2 α-globin chains and 2 β-globin chains, arranged as two dimers of αβ. In Sickle Cell Disease, both β-globin chains are altered in the dimers (αβS/αβS). Q3: Which level of structure does the αβ/αβ and αβS/αβS in HbA and HbS describe?arrow_forwardConsidering that we are all made up of the same 4 nucleotides in our DNA, the same 4 nucleotides in our RNA, and the same 20 amino acids in our proteins, why are we so different from each other? For example, why do some people have sickle cell anemia and others don't?arrow_forwardOne molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant). (Please provide clear and sufficient explanation for the question, thank you!)arrow_forward
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