L20 462a_hemoglobin3_lec20_2012

L20 462a_hemoglobin3_lec20_2012

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Unformatted text preview: stability
 1. Aggrega:on: sickle cell hemoglobin (HbS) 
 βE6V (change of normal β residue 6 from Glu to Val) Residue 6 is at surface of β chain. Hydrophobic Val 6 on β subunit of 1 tetramer sticks to patch on T state β subunit of another tetramer. Residues in pocket, patch T state but not R state HbS has a hydrophobic “pocket” on β surface, present also on normal deoxyHb β, that the βS Val 6 “knob” sticks to. Berg, Tymoczko & Stryer, Biochemistry, 6th ed, Fig. 7-25 So tetramers of deoxy (but not oxy) HbS aggregate HbS aggrega:on 
 Hydrophobic pocket Each tetramer has 2 β subunits = 2 knobs, 2 hydro...
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This note was uploaded on 01/22/2014 for the course BIOC 462A taught by Professor Ziegler,baldwin during the Winter '08 term at University of Arizona- Tucson.

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