Hemoglobin In Red Blood Cells

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CHAPTER I
INTRODUCTION

Background and Significance
Sickle cell disease (SCD) is an inherited red blood cell disorder that is present at birth and is often more prevalent amongst African Americans.1 In order to inherit SCD, a person must inherit two abnormal hemoglobin genes, one from each parent. Hemoglobin is a protein found in red blood cells that is responsible for absorbing oxygen in the lungs and transporting it throughout the body.13 Proteins typically have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure of a protein, such as hemoglobin, helps determine the three dimensional structure and properties of the protein. Primary structure is determined by the amino acid sequence; if the sequence is abnormal than the protein will not function properly.14 Amino acids are linked
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This secondary structure involves the folding and/or coiling of individual polypeptide chains into either alpha helices or beta pleated sheets. Hemoglobin consists of four polypeptide chains, forming two alpha helices and two beta pleated sheets. The bonds and forces holding these secondary structures into an organized, three dimensional shape gives hemoglobin its tertiary structure. The quaternary structure of hemoglobin refers to the entire structure of the protein macromolecule formed by the interaction between multiple polypeptide chains. Hemoglobin consists of two alpha helices and two beta bleated sheets, known as globular subunits.15 As Figure 1 depicts, sickle cell disorder results from a single nucleotide mutation which leads to the substitution of glutamic acid by valine in the beta globular subunits, upsetting the typical protein structure which leads to the

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