Lecture11 - Lecture 11 2/02/09 Background reading: Garrett...

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Lecture 11 2/02/09 Background reading: Garrett and Grisham: Chapter 15: Pages 498 - 500 Assignment: Segel Read Pages 86 - 90 Outline: Allosteric behavior of hemoglobin Hemoglobin as a blood buffer
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Allosteric behavior of hemoglobin In the last lecture we had seen that the binding curve of hemoglobin to oxygen is sigmoidal. When the α-subunit binds to oxygen, it causes a conformational change in the protein that pulls the iron in the β-subunit into the plane of the heme, pulling the proximal histidine (His 146) with it. Β 2 -chain carboxyl terminal end H146 α 1 -chain amino-terminal end α 2 -chain β 1 -chain amino-terminal end carboxyl terminal end K40 H146 K40
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The movement of His 146 is thought to play a key role in transmitting structural changes to the interfaces between the subunits where they rupture the interchain salt links and the conformation shifts from the T form to a relaxed ® form. Thus a structural change occurs in the hemoglobin and the pockets on the β-subunits open and are able to bind to oxygen. It is thought that the number of salt linkages that are broken during binding
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This note was uploaded on 02/21/2009 for the course BIS BIS102 taught by Professor Hilt during the Winter '08 term at UC Davis.

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Lecture11 - Lecture 11 2/02/09 Background reading: Garrett...

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