Final Answers - 2007 - FINAL - 2007 - KEY Friday, December...

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Unformatted text preview: FINAL - 2007 - KEY Friday, December 14, 2007 3:30 PM FINAL-Key Page 1 FINAL-Key Page 2 FINAL-Key Page 3 FINAL-Key Page 4 FINAL-Key Page 5 FINAL-Key Page 6 FINAL-Key Page 7 FINAL-Key Page 8 FINAL-Key Page 9 FINAL-Key Page 10 FINAL-Key Page 11 FINAL-Key Page 12 FINAL-Key Page 13 FINAL-Key Page 14 FINAL-Key Page 15 FINAL-Key Page 16 FINAL-Key Page 17 FINAL-Key Page 18 FINAL-Key Page 19 FINAL-Key Page 20 FINAL-Key Page 21 FINAL-Key Page 22 The allosteric oxygen (O 2 ) binding properties of hemoglobin (Hb) arise from the interaction of oxygen with the iron atom of the heme prosthetic groups. These interactions in turn change the tertiary and quaternary structures of the protein. When oxygen binds to an iron atom of deoxyhemoglobin it pulls the iron atom into the plane of the heme. Since the iron is also bound to a histidine, this residue is also pulled toward the plane of the heme ring. The conformational change at the histidine is transmitted throughout the peptide backbone resulting in a significant change in...
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Final Answers - 2007 - FINAL - 2007 - KEY Friday, December...

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