PPT-Hemoglobin, an Allosteric Protein
Author : giovanna-bartolotta | Published Date : 2016-07-12
Stryer Short Course Case Study Hemoglobin Structure Quaternary h eme group Function Oxygen binding Physiology oxygen delivery from lungs to tissue Myoglobin no
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Hemoglobin, an Allosteric Protein: Transcript
Stryer Short Course Case Study Hemoglobin Structure Quaternary h eme group Function Oxygen binding Physiology oxygen delivery from lungs to tissue Myoglobin no quaternary structure stores oxygen in muscle tissue. . Electrophoresis. Electrophoresis. Electrophoresis is a means of separating hemoglobin's. . . It depends on the migration of the hemoglobin molecules dissolved in a buffer on, or in, a supporting medium when an electric current is passed through them. b. d. g. a. a. Chromosome 16. Chromosome 11. 25%. 25%. a. a. b. d. g. 25%. 25%. 48%. 48%. 1.5%. 0.5%. 1.5%. 0.5%. Hemoglobin synthesis. a. a. a. a. a. a. b. g. d. b. d. g. HbA. HbF. HbA. 2. 98%. ~1%. Electrophoresis. Electrophoresis. Electrophoresis is a means of separating hemoglobin's. . . It depends on the migration of the hemoglobin molecules dissolved in a buffer on, or in, a supporting medium when an electric current is passed through them.. . A/Prof Gilda Tachedjian. Retroviral Biology and Antivirals Laboratory. Centre for Biomedical Research. Burnet Institute. Discover Novel Allosteric Inhibitors of HIV-1 RT. . Polymerase active site. Hemoglobin. Hemoglobin is the protein molecule in red blood cells that carries oxygen from the lungs to the body's tissues and returns carbon dioxide from the tissues back to the lungs.. Hemoglobin. Hemoglobin (. The ribbon model represents the tertiary structure of the polypeptide chain that forms myoglobin, a globular protein.. Learning Goal . Describe the tertiary and quaternary structures of a protein.. Tertiary Structure. Hemoglobin variant trait is common and can occur in any race or ethnicity You may have heard of sickle cell trait before while not exactly the same sickle cell trait and hemoglobin variant trait are s Adult male: 4.6 – 6 million. Adult female: 4.2 – 5 million. Red blood cells are: . Tiny, flexible biconcave discs. Lacks a nucleus. Can bend when going through tiny capillaries. RBC’s are constantly manufactured. globin. chains. Abnormalities in these proteins are referred to as . hemoglobinopathies. Two hemoglobin gene clusters are involved in the production of hemoglobin and are located at the end of the short arm of chromosomes 16 and 11, respectively. . . By – . Dr. Sunita Mittal. Learning Objectives. ▪. Iron metabolism . ▪. Hemoglobin catabolism (Fate of old RBCs) . ▪. Prehepatic. Jaundice. Iron . (Fe. +2. ) Metabolism. Iron is essential for . Hemoglobin E trait is common and can occur in any race or ethnicity. It is most common in individuals of Southeast Asian descent. You may have heard of sickle cell trait before, while not exactly the Hemoglobin. . Found in the RBC.. Responsible for carrying oxygen to all cells in the body.. Also binds to carbon dioxide and carries it to the lungs from the cells to be released.. Buffer against change in [H. Allostery. :. Glycogen Phosphorylase:. Control by . Allostery. & Phosphorylation. Glycogen. (n). +. P. i. +. Glycogen. (n-1). . (more active). Enzyme Regulation. Control by . Allostery. :. Glycogen Phosphorylase:. What is Hemoglobin?. Hemoglobin is a protein in red blood cells that binds to oxygen in the lungs and carries the oxygen to the tissues.. What is Hemoglobin?. Hemoglobin has a . tetrameric . structure; it is made up of four subunits (2 α chains and 2 β chains) bound together..
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