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Chapter 5

Chapter 5. Chem 341 Suroviec Fall 2013. I. Introduction. Every protein has a unique 3-D structure. II. Myoglobin. Small intercellular protein. A. Heme group. Heme contains 4 pyrrole groups

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Chapter 5

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  1. Chapter 5 Chem 341 Suroviec Fall 2013

  2. I. Introduction • Every protein has a unique 3-D structure

  3. II. Myoglobin • Small intercellular protein

  4. A. Heme group • Heme contains 4 pyrrole groups • Fe(II) atom at the center is coordinated by the 4 porphyrin N atoms and one N from a His side chain

  5. B. Equilibrium of O2 binding • Myoglobin binding of O2 is simple equilibrium

  6. C. Binding Curve Steepness of hyperbola increases as K decreases

  7. III. Hemoglobin Structure & Mechanism • 4 polypeptide chains • 2  subunits • 2  subunits

  8. III. Hemoglobin Structure & Mechanism • Oxygenation causes extensive quaternary structural changes • Oxy- and Deoxy- Hb have different forms

  9. A. Binding of O2 • T-state (deoxy) • R-state (oxy) In T state (blue) Fe(II) located 0.6 Å out of heme plane When O2 binds Fe-N porphyrin bonds contract and Fe(II) moves in plane (red)

  10. B. 2 Stable Positions • Difference between T and R occur at 1-2 and 2-1 interface

  11. Protect Fe(II) His attached to backside of porphyrin C. Role of Globin in Binding of O2

  12. D. Relative Stability of T and R • With no O2 present: T more stable • With O2 present: R more stable

  13. V. Hemoglobin binding and pH • Effect of pH on Hb transport • Lung pH = 7.6 • Blood pH = 7.2 • pO2 in tissues = 30 torr • pO2 in lungs = 95 torr

  14. Bohr Effect

  15. VI. 2 – 3 Bis-phosphoglycerate • Red blood cells use BPG to fine tune hemoglobin function

  16. VII. Abnormal Hemoglobins • Sickle Cell Anemia • Deoxyhemoglobin S forms insoluble filaments that deform red blood cells • Rigid sickle shaped cells cannot pass through the capillaries • Results in tissue death: lack of oxygen • Mutant hemoglobin where hemoglobin S contains Val instead of Glu at the 6th position of the  chain • Causes polymerization of hemoglobins

  17. VIII. Structural Proteins Typical eukaryotic cells have 3 types of cytoskeletal proteins that form fibers

  18. A. Microfilaments • Made of actin • Network of microfilaments support plasma membrane

  19. B. Microfilaments extend/retract • Polymerization of actin monomers is reversible process so the polymer undergoes constant shrinking and growing as subunits add to and dissociate from one or both ends of the microfilaments

  20. C. Microtubules • Microtubules are cytoskeletal fibers built from globular protein subunits • Microtubules can assemble and disassemble on a time scale that allow the cell to rapidly change shape in response to external or internal stimuli

  21. D. -Keratin • Intermediate filaments are structural proteins • Chemically un-reactive • Component of hair, horns, nails and feathers • -helix shape, but exhibits smaller than expected spacing - due to coiled coil structure

  22. E. Collagen • Most abundant animal protein • Major stress-bearing components of connective tissues (bone, teeth, tendons) • Has distinct amino acid composition • Every 3rd amino acid = glycine

  23. Cross-linking between fibrils also increases insolubility Can’t be S-S bonds Cross-link between Lys and His chains using Lysyl oxidase Tends to occur near termini E. Collagen

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