Campbell Biology (10th Edition)
Campbell Biology (10th Edition)
10th Edition
ISBN: 9780321775658
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Chapter 23, Problem 8TYU
Summary Introduction

To write: A short essay to explain the molecular and cellular events leading to the heterozygotes individuals in sickle cell trait leading to the individual and population levels of biological organisation. .

Introduction:

Sickle cell disease is the most commonly occurring recessive inherited disorder found in African – Americans with an incidence of 1/400 and a carrier frequency of 1/10. It is caused due to the sickle cell allele that results in the structural and functional abnormality in normal haemoglobin. A point mutation that causes the substitution of glutamic acid by valine at 6th position of β-globin chain of haemoglobin is the main cause. The homozygous recessive individuals suffer severely from the disease; however the heterozygous carriers have the benefit of killing the malarial parasites in malaria rich regions of the World.

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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
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.
Normal Hgb is referred to as HbA and contains 4 subunits, 2 a-globin chains and 2 B-globin chains, arranged as two dimers of aß. In Sickle Cell Disease, both B-globin chains are altered in the dimers (aßS/aßS). Q3: Which level of structure does the aß/aß and aßS/aßS in HbA and HbS describe?
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