Conformational changes in oxyhemoglobin C (Glu beta 6-->Lys) detected by spectroscopic probing.
Hemoglobin C (Glu beta 6-->Lys) shares with hemoglobin S (Glu beta 6-->Val) the site of mutation, but with different consequences: deoxyHbS forms polymers, whereas oxyHbC readily forms crystals. The molecular mechanism for this property of oxyHbC is unknown. Since no detailed oxyHbC crystal structural information exists, spectroscopic probing is used in this study to investigate possible solution-phase conformational changes in HbC compared with HbA. Intrinsic fluorescence combined with UV resonance Raman data demonstrate a weakening of the Trp beta 15-Ser beta 72 hydrogen bond that most likely leads to a displacement of the A helix away from the E helix.
Hirsch
R E
RE
Department of Medicine, Montefiore Medical Center, Bronx, New York, USA.
Lin
M J
MJ
Vidugiris
G J
GJ
Huang
S
S
Friedman
J M
JM
Nagel
R L
RL
Vidugirus
G V
GV
D018698:Glutamic Acid / Q000737:chemistry*; D006801:Humans; D008239:Lysine / Q000737:chemistry*; D010108:Oxyhemoglobins / Q000737:chemistry*; D011487:Protein Conformation; D013057:Spectrum Analysis
D010108:Oxyhemoglobins; D018698:Glutamic Acid; D008239:Lysine