L20 462a_hemoglobin3_lec20_2012

L20 462a_hemoglobin3_lec20_2012

Info iconThis preview shows page 1. Sign up to view the full content.

View Full Document Right Arrow Icon
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: stability
of
R
state
or
T
state
 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...
View Full Document

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.

Ask a homework question - tutors are online