TY - JOUR
T1 - Conformational changes in oxyhemoglobin C (Gluβ6 → Lys) detected by spectroscopic probing
AU - Hirsch, Rhoda Elison
AU - Lin, Margaret J.
AU - Vidugirus, Gediminas V.A.
AU - Huang, Shuocai
AU - Friedman, Joel M.
AU - Nagel, Ronald L.
PY - 1996/1/5
Y1 - 1996/1/5
N2 - Hemoglobin C (Glu β6 → Lys) shares with hemoglobin S (Gluβ6 → 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 Trpβ15-Serβ72 hydrogen bond that most likely leads to a displacement of the A helix away from the E helix.
AB - Hemoglobin C (Glu β6 → Lys) shares with hemoglobin S (Gluβ6 → 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 Trpβ15-Serβ72 hydrogen bond that most likely leads to a displacement of the A helix away from the E helix.
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U2 - 10.1074/jbc.271.1.372
DO - 10.1074/jbc.271.1.372
M3 - Article
C2 - 8550589
AN - SCOPUS:0030043597
SN - 0021-9258
VL - 271
SP - 372
EP - 375
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 1
ER -