06 Hemoglobin - B iochemis ry E duca ion Department of...

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Unformatted text preview: B iochemis ry E duca ion Department of iochemistry & Molecular iology University of New Mexico BIOC 423 Int oducto y Biochemist y Myoglobin and Hemoglobin: Oxygen- binding proteins OBJECTIVES Be able to define and explain the terms: prosthetic group, apoprotein, protoporphyrin, cooperative binding, Bohr effect, allosterism Understand the coordination chemistry of Iron as it pertains to the binding of oxygen by hemoglobin and myoglobin. Be able to describe the three-dimensional structure of hemoglobin and how it changes with the oxygenization-deoxygenization cycle. Be able to explain the functional significance of the hemoglobin oxygen- binding curve. Understand how H + (Bohr effect), CO 2 , and 2,3 Diphosphoglycerate (2,3 DPG, or 2,3 BPG) affect oxygen binding by hemoglobin. Be able to compare and contrast the structure, overall function, and oxygen binding properties of hemoglobin and myoglobin. Be able to draw and interpret oxygen-binding curves Be able to describe how hemoglobin structure is perfect for the binding and, just as important, the releasing of oxygen OUTLINE The oxygen binding problem Myoglobin Prosthetic Groups Apoproteins vs. Holoproteins Heme structure Oxygen binding site Measurement of ligand binding Problems with using Mb to transport oxygen Hemoglobin Measurement of oxygen binding Cooperativity Concerted and Sequential models of oxygen binding Allosteric Regulation Bohr effect 2,3-BPG Carbon dioxide LECTURE The study of how proteins function is a major part of the discipline of biochemistry. Biologically proteins solve all sorts of problems that are both structural and functional. In this course we already have had an introduction to the structural function of proteins in our discussions of silk and collagen. We have started talking about enzymes with our discussion of proteolytic enzymes and will spend a great deal of time on the enzymic activities of proteins when we discuss metabolism. Answering the question how do proteins do what they do? is an interesting study that unfortunately in this survey class we do not have time to go into depth on each class of protein. In this class we will be limited to how hemoglobin functions as our example protein. The student should also read about structural proteins, ligand binding proteins and enzymes, which we will meet later in the course. Myoglobin and hemoglobin are oxygen-binding proteins which provide specific examples of the relationship between protein conformation and protein function, the role(s) of individual amino acids in proteins, and the roles of noncovalent interactions in protein function. Myoglobin and hemoglobin have been selected because we know a lot about the 3-D structure of these proteins from X-ray diffraction studies and because of their relationship to issues of health and disease. In addition, these proteins will introduce the important concept of allosterism....
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06 Hemoglobin - B iochemis ry E duca ion Department of...

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