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Biomolecules

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Chapter 4: Protein Function
Chapter 7, Voet, Voet & Pratt * Link between protein structure and physiological function * Focus on myoglobin and hemoglobin * Both proteins reversibly bind to O2 * Extremely well-studied examples of structure/function relationships * Behavior is a model for many other proteins, especially metabolic enzymes
Learning Objectives * Compare myoglobin and hemoglobin * Structures * Properties * O2 binding characteristics * Understand structural basis for hemoglobin’s O2 binding characteristics * Relate these characteristics to physiological role of hemoglobin * Understand biochemical basis of diseases/adaptations involving hemoglobin
O2 Binding Proteins: Myoglobin (Mb) * Is a Monomeric protein * A single polypeptide * Has 153 residues, most are members of 8 α-helices (A-H) * Is a globular protein * Has 1 O2 binding site; reversibly binds O2 * O2: low solubility in water; diffusion through tissue is ineffective past a few mm
Myoglobin Contains a Heme Prosthetic Group * Figure 7.2, 7.3 * Not responsible for knowing the structure of heme, just need to know that it contains iron which gives it is specific O2 binding properties * The color properties of this group changes due to the presence of oxygen * Red when there is oxygen is bound; blue when oxygen is not bound
Myoglobin’s O2 Binding Curve is Hyperbolic * Consider the chemical equation for O2 reversibly bind with Mb:
Mb + O2 MbO2 * The dissociation constant for this reaction is:

K= MbO2MbO2
But this relationship is not helpful experimentally, so we need to reformulate it in terms that we can measure * Begin by writing an equation that gives us a measure of the fraction of binding sites that are occupied
YO2= MbO2Mb+MbO2 * After some algebra, obtain

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