Unit 3: Seminar Sickle Cell Anemia. Types of Biomolecules Figure 2-17 Molecular Biology of the Cell...
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Transcript of Unit 3: Seminar Sickle Cell Anemia. Types of Biomolecules Figure 2-17 Molecular Biology of the Cell...
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Unit 3: Seminar
Sickle Cell Anemia
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Types of Biomolecules
Figure 2-17 Molecular Biology of the Cell (© Garland Science 2008)
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Amino Acids
Amino acids are the basic subunits of proteins.
Each amino acid contains the following parts:
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Amino Acids
20 different types of amino acids typically use in proteins
The “R” group is what makes each unique
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Polypeptides
Multiple amino acids are joined together through peptide bonds to form polypeptides.
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Protein Structure
The function of a protein is related to its structure.
There are 4 levels of protein structure:
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Protein Structure
The function of a protein is related to its structure.
There are 4 levels of protein structure: Primary Secondary Tertiary Quaternary
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Primary Protein Structure
Primary structure = the linear sequence of amino acids
Aminoacid 1
Aminoacid 2
Aminoacid 3
Aminoacid 4
Peptidebond
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Secondary Protein Structure
Secondary structure = folding of polypeptides into alpha-helices or beta-sheets
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Tertiary Structure
Tertiary structure = 3-dimensional folded “globular” structure
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Quaternary Structure
Quaternary structure = combination of multiple folded polypeptides
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Sickle Cell Anemia: Molecular Basis
A single nucleotide polymorphism in the gene for the beta-subunit of hemoglobin
Results in a single amino acid change:
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Sickle Cell Anemia: Molecular Basis
A single nucleotide polymorphism in the gene for the beta-subunit of hemoglobin
Results in a single amino acid change:
Glu
Val
. . . .
. . . .
HbA:
HbS:
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Sickle Cell Anemia: Molecular Basis
Normal hemoglobin = the major protein which fills red blood cells
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Sickle Cell Anemia: Molecular Basis
Normal hemoglobin = the major protein which fills red blood cells Carries oxygen from the lungs to body tissues Carries carbon dioxide away from body tissues to the lungs
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Sickle Cell Anemia: Molecular Basis
Normal hemoglobin = the major protein which fills red blood cells Carries oxygen from the lungs to body tissues Carries carbon dioxide away from body tissues to the lungs
Oxygenated: Deoxygenated:
Normal hemoglobin floats free in the RBC.
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Sickle Cell Anemia: Molecular Basis
Normal hemoglobin = the major protein which fills red blood cells Carries oxygen from the lungs to body tissues Carries carbon dioxide away from body tissues to the lungs
Oxygenated: Deoxygenated:
Normal hemoglobin floats free in the RBC.
HbS sticks together when it becomes deoxygenated, forming long, rigid strands.
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Normal vs. Sickle Cell
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Sickle Cell Disease
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Sickle Cell Disease
Consequences: Anemia (low hemoglobin) due to removal of abnormal RBCs
Fatigue Shortness of breath Enlarged spleen
Vaso-occlusion (blockage of blood vessels) Pain Necrosis Stroke Renal failure
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Sickle Cell Gene Distribution
Why is the sickle cell gene (HbS) so prevalent in certain areas of the world?
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Sickle Cell Genetics
Each person has two copies of the gene for beta-hemoglobin A = “normal” dominant form S = sickle cell, recessive form
AA normal phenotypeAs sickle cell carrierSs sickle cell disease
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Sickle Cell and Malaria
Sickle cell has higher prevalence in regions where malaria is endemic.
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HbS and the “Heterozygote Advantage”
Sickle cell actually has a protective effect against malaria!
AA Asssor
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Sickle Cell Anemia: Treatment
Prevention of sickle cell crisis episodes
Management of symptoms
Bone marrow transplant
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Unit 4
Discussion topic: Antibiotics
Lab Project #2: Continue data collection
Test #1: 30 multiple choice questions on units 1-4