Lecture_27_2011

Lecture_27_2011 - stoichiometry because the tetrameric Hb...

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Introduction to Biophysics Lecture 27 Allostery - Hemoglobin
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Hemoglobin http://en.wikipedia.org/wiki/Image:Hemoglobin_t-r_state_ani.gif Myoglobin
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Hill plot
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Modulation of O 2 binding Protons, carbon dioxide, and chloride ions, as well as the metabolite 2,3-bisphosphoglycerate (or BPG), all affect the binding of O 2 by hemoglobin. The pH decrease enhances dissociation of O 2 from hemoglobin. The binding of BPG to Hb promotes the release of O 2 . Erythrocytes (red blood cells) normally contain about 4.5 m M BPG, a concentration equivalent to that of tetrameric hemoglobin molecules. Interestingly, this equivalence is maintained in the Hb:BPG binding
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Unformatted text preview: stoichiometry because the tetrameric Hb molecule has but one binding site for BPG. Reading Nelson 9.6, Problems: your turn 9N (page 377), example on page 223 Derive the Gibbs–Helmholtz equation. The Gibbs–Helmholtz equation is a thermodynamic equation useful for calculating changes in the Gibbs energy of a system as a function of temperature at constant pressure. It is named after Josiah Willard Gibbs and Hermann von Helmholtz: The equation states that the change in the G/T ratio at constant pressure as a result of an infinitesimally small change in temperature is a factor (H/T 2 )....
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This note was uploaded on 12/09/2011 for the course PHYS 570 taught by Professor Staff during the Fall '08 term at Purdue.

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Lecture_27_2011 - stoichiometry because the tetrameric Hb...

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